Structural biology of the multidrug and toxic compound extrusion superfamily transporters

Xenobiotic and metabolite extrusion is an important process for the proper functions of cells and their compartments, including acidic organelles. MATE (multidrug and toxic compound extrusion) is a large family of secondary active transporters involved in the transport of various compounds across ce...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biochimica et biophysica acta. Biomembranes Jg. 1862; H. 12; S. 183154
Hauptverfasser: Kusakizako, Tsukasa, Miyauchi, Hirotake, Ishitani, Ryuichiro, Nureki, Osamu
Format: Journal Article
Sprache:Englisch
Veröffentlicht: Netherlands Elsevier B.V 01.12.2020
Schlagworte:
ISSN:0005-2736, 1879-2642, 1879-2642
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Abstract Xenobiotic and metabolite extrusion is an important process for the proper functions of cells and their compartments, including acidic organelles. MATE (multidrug and toxic compound extrusion) is a large family of secondary active transporters involved in the transport of various compounds across cellular and organellar membranes, and is present in the three domains of life. The major substrates of the bacterial MATE transporters are cationic compounds, including clinically important antibiotics, and thereby MATE transporters confer multi-drug resistance to pathogenic bacteria. The plant MATE transporters are important for the accumulation of various metabolites in organelles, including vacuoles. The human MATE transporters are expressed in the brush-border membrane of the kidney, and are involved in the clearance of cationic drugs from the body. During the past decade, progress in structural biology has clarified the transport mechanism of these MATE transporters in atomic detail. The present review summarizes the reported structures of MATE family transporters, along with their structure-guided functional analyses. This integrated view of the structures of MATE transporters provides novel insights into their transport mechanism. •MATE (multidrug and toxic compound extrusion) is a large family of secondary active transporters.•MATE is involved in the transport of various xenobiotics and metabolites across cellular and organellar membranes.•The present review summarizes the reported structures of MATE family transporters.•The integrated view of the structures of MATE transporters provides novel insights into their transport mechanism.
AbstractList Xenobiotic and metabolite extrusion is an important process for the proper functions of cells and their compartments, including acidic organelles. MATE (multidrug and toxic compound extrusion) is a large family of secondary active transporters involved in the transport of various compounds across cellular and organellar membranes, and is present in the three domains of life. The major substrates of the bacterial MATE transporters are cationic compounds, including clinically important antibiotics, and thereby MATE transporters confer multi-drug resistance to pathogenic bacteria. The plant MATE transporters are important for the accumulation of various metabolites in organelles, including vacuoles. The human MATE transporters are expressed in the brush-border membrane of the kidney, and are involved in the clearance of cationic drugs from the body. During the past decade, progress in structural biology has clarified the transport mechanism of these MATE transporters in atomic detail. The present review summarizes the reported structures of MATE family transporters, along with their structure-guided functional analyses. This integrated view of the structures of MATE transporters provides novel insights into their transport mechanism. •MATE (multidrug and toxic compound extrusion) is a large family of secondary active transporters.•MATE is involved in the transport of various xenobiotics and metabolites across cellular and organellar membranes.•The present review summarizes the reported structures of MATE family transporters.•The integrated view of the structures of MATE transporters provides novel insights into their transport mechanism.
Xenobiotic and metabolite extrusion is an important process for the proper functions of cells and their compartments, including acidic organelles. MATE (multidrug and toxic compound extrusion) is a large family of secondary active transporters involved in the transport of various compounds across cellular and organellar membranes, and is present in the three domains of life. The major substrates of the bacterial MATE transporters are cationic compounds, including clinically important antibiotics, and thereby MATE transporters confer multi-drug resistance to pathogenic bacteria. The plant MATE transporters are important for the accumulation of various metabolites in organelles, including vacuoles. The human MATE transporters are expressed in the brush-border membrane of the kidney, and are involved in the clearance of cationic drugs from the body. During the past decade, progress in structural biology has clarified the transport mechanism of these MATE transporters in atomic detail. The present review summarizes the reported structures of MATE family transporters, along with their structure-guided functional analyses. This integrated view of the structures of MATE transporters provides novel insights into their transport mechanism.Xenobiotic and metabolite extrusion is an important process for the proper functions of cells and their compartments, including acidic organelles. MATE (multidrug and toxic compound extrusion) is a large family of secondary active transporters involved in the transport of various compounds across cellular and organellar membranes, and is present in the three domains of life. The major substrates of the bacterial MATE transporters are cationic compounds, including clinically important antibiotics, and thereby MATE transporters confer multi-drug resistance to pathogenic bacteria. The plant MATE transporters are important for the accumulation of various metabolites in organelles, including vacuoles. The human MATE transporters are expressed in the brush-border membrane of the kidney, and are involved in the clearance of cationic drugs from the body. During the past decade, progress in structural biology has clarified the transport mechanism of these MATE transporters in atomic detail. The present review summarizes the reported structures of MATE family transporters, along with their structure-guided functional analyses. This integrated view of the structures of MATE transporters provides novel insights into their transport mechanism.
Xenobiotic and metabolite extrusion is an important process for the proper functions of cells and their compartments, including acidic organelles. MATE (multidrug and toxic compound extrusion) is a large family of secondary active transporters involved in the transport of various compounds across cellular and organellar membranes, and is present in the three domains of life. The major substrates of the bacterial MATE transporters are cationic compounds, including clinically important antibiotics, and thereby MATE transporters confer multi-drug resistance to pathogenic bacteria. The plant MATE transporters are important for the accumulation of various metabolites in organelles, including vacuoles. The human MATE transporters are expressed in the brush-border membrane of the kidney, and are involved in the clearance of cationic drugs from the body. During the past decade, progress in structural biology has clarified the transport mechanism of these MATE transporters in atomic detail. The present review summarizes the reported structures of MATE family transporters, along with their structure-guided functional analyses. This integrated view of the structures of MATE transporters provides novel insights into their transport mechanism.
ArticleNumber 183154
Author Miyauchi, Hirotake
Ishitani, Ryuichiro
Nureki, Osamu
Kusakizako, Tsukasa
Author_xml – sequence: 1
  givenname: Tsukasa
  surname: Kusakizako
  fullname: Kusakizako, Tsukasa
– sequence: 2
  givenname: Hirotake
  surname: Miyauchi
  fullname: Miyauchi, Hirotake
– sequence: 3
  givenname: Ryuichiro
  surname: Ishitani
  fullname: Ishitani, Ryuichiro
  email: ishitani@bs.s.u-tokyo.ac.jp
– sequence: 4
  givenname: Osamu
  surname: Nureki
  fullname: Nureki, Osamu
  email: nureki@bs.s.u-tokyo.ac.jp
BackLink https://www.ncbi.nlm.nih.gov/pubmed/31866287$$D View this record in MEDLINE/PubMed
BookMark eNqFkE1rFTEUhoO02NvqPxDJ0s1ck0xmJnEhSKkfUOhCXbgKmeSk5jIzGfNRev99U6bduNDV4cD7vPA-5-hkCQsg9IaSPSW0f3_Yj6OeYd4zQuWeipZ2_AXaUTHIhvWcnaAdIaRr2ND2Z-g8pQOpGGfdS3TWUtH3TAw79Ot7jsXkEvWERx-mcHvEweH8G_BcpuxtLLdYLxbncO8NNmFeQ6kv3Fcu-bDgVFaITs9-OuIc9ZLWEDPE9AqdOj0leP10L9DPz1c_Lr821zdfvl1-um4MH3huzChkbzS1nXCuI5YZzSnXRkrG-lZKy8C1WljtjHNyoGYcxdgLsANxA6-zL9C7rXeN4U-BlNXsk4Fp0guEkhRr26pBdh2t0bdP0TLOYNUa_azjUT3rqIEPW8DEkFIEp4zPOteZdZmfFCXq0b06qM29enSvNvcV5n_Bz_3_wT5uGFRJdx6iSsbDYsD6CCYrG_y_Cx4AaZuiAw
CitedBy_id crossref_primary_10_1007_s00253_020_10873_9
crossref_primary_10_3390_agronomy12040878
crossref_primary_10_1007_s13562_021_00743_4
crossref_primary_10_1080_14756366_2022_2063282
crossref_primary_10_3390_microorganisms8091350
crossref_primary_10_1111_mec_17775
crossref_primary_10_1073_pnas_2501933122
crossref_primary_10_3390_membranes12020206
crossref_primary_10_3390_pathogens14070648
crossref_primary_10_1371_journal_pone_0303065
crossref_primary_10_3390_antibiotics11101287
crossref_primary_10_1124_molpharm_122_000604
crossref_primary_10_1002_1873_3468_14136
crossref_primary_10_1186_s12866_024_03682_x
crossref_primary_10_3389_fpls_2022_867731
crossref_primary_10_3389_fpls_2022_1021088
crossref_primary_10_1080_21688370_2021_2013695
crossref_primary_10_1007_s00203_023_03731_5
crossref_primary_10_1016_j_biochi_2022_07_019
crossref_primary_10_1080_00498254_2021_1875516
crossref_primary_10_1016_j_gene_2023_147734
crossref_primary_10_1073_pnas_2107335118
crossref_primary_10_1146_annurev_biochem_040320_105145
crossref_primary_10_1007_s10068_022_01157_1
crossref_primary_10_3390_plants13182586
crossref_primary_10_3390_antibiotics11040520
crossref_primary_10_1016_j_ijbiomac_2024_139115
crossref_primary_10_1016_j_ejmech_2024_117197
crossref_primary_10_1007_s10709_023_00186_w
crossref_primary_10_3390_genes14111979
crossref_primary_10_3390_microbiolres16030067
crossref_primary_10_1111_pce_15092
crossref_primary_10_3390_microorganisms12122433
crossref_primary_10_1098_rsob_240310
crossref_primary_10_3390_ijms22073531
crossref_primary_10_1016_j_jmb_2021_167005
crossref_primary_10_1007_s12088_024_01384_6
crossref_primary_10_1016_j_bioorg_2025_108194
crossref_primary_10_1016_j_biotechadv_2025_108519
crossref_primary_10_1007_s11783_021_1466_7
crossref_primary_10_1007_s42250_022_00414_4
crossref_primary_10_1016_j_jmb_2021_166959
crossref_primary_10_1038_s42003_021_02081_6
crossref_primary_10_3389_fmicb_2025_1454510
crossref_primary_10_3390_biomedicines10092219
crossref_primary_10_3390_microorganisms10020382
crossref_primary_10_3390_genes13020228
crossref_primary_10_1146_annurev_micro_041522_092911
crossref_primary_10_1016_j_biotechadv_2025_108686
crossref_primary_10_1002_cpt_2627
crossref_primary_10_1016_j_biopha_2021_112009
crossref_primary_10_3390_membranes13060568
crossref_primary_10_1128_spectrum_01128_24
crossref_primary_10_1016_j_tim_2025_04_012
crossref_primary_10_1016_j_str_2022_05_008
crossref_primary_10_1016_j_jbc_2021_100262
crossref_primary_10_1016_j_bbrc_2024_150821
crossref_primary_10_1073_pnas_2506170122
crossref_primary_10_2478_am_2022_0009
crossref_primary_10_2478_am_2022_009
crossref_primary_10_3389_fpls_2021_758202
crossref_primary_10_1016_j_str_2024_05_004
crossref_primary_10_1155_2021_3663315
Cites_doi 10.1128/JB.186.1.262-265.2004
10.1016/j.tips.2006.09.001
10.1016/j.jmb.2018.03.012
10.1046/j.1365-2958.1999.01162.x
10.1128/AAC.46.9.3050-3053.2002
10.1016/j.bbapap.2008.11.012
10.1128/AAC.00475-08
10.3390/molecules180910514
10.1124/jpet.111.184986
10.1016/j.sbi.2015.07.015
10.1016/j.bpj.2016.01.027
10.1128/JB.187.5.1552-1558.2005
10.1128/JB.184.2.572-576.2002
10.1111/j.1574-6968.2001.tb10847.x
10.1371/journal.pgen.1003120
10.1146/annurev-biochem-060815-014520
10.1152/ajpcell.00504.2007
10.5511/plantbiotechnology.14.0904a
10.1038/s41467-017-01541-0
10.1111/j.1348-0421.2005.tb03690.x
10.1038/nature09408
10.1128/AAC.49.5.1865-1871.2005
10.1093/jxb/erp312
10.1074/jbc.M116.728618
10.1128/AAC.49.10.4362-4364.2005
10.1074/jbc.M113.546770
10.1016/j.bcp.2007.03.004
10.1104/pp.107.097162
10.1016/j.str.2018.10.004
10.1073/pnas.0506483102
10.1681/ASN.2006030205
10.1016/j.resmic.2018.01.001
10.1128/AAC.42.7.1778
10.1111/j.1365-313X.2008.03696.x
10.1016/j.str.2017.07.009
10.1038/ncomms8995
10.1128/JB.182.23.6694-6697.2000
10.1038/nsmb.2687
10.1074/jbc.M108777200
10.1016/j.phrs.2016.06.002
10.1073/pnas.0812512106
10.1073/pnas.1904210116
10.1111/j.1348-0421.2003.tb03379.x
10.1073/pnas.1802080115
10.1038/nature12014
10.1073/pnas.1219901110
10.1021/bi2015184
10.1128/AAC.49.5.1857-1864.2005
10.1073/pnas.1802417115
10.1104/pp.108.132811
10.1016/j.bcp.2007.04.010
10.1105/tpc.106.046029
10.1146/annurev-biophys-060414-033901
ContentType Journal Article
Copyright 2019 The Author(s)
Copyright © 2019 The Author(s). Published by Elsevier B.V. All rights reserved.
Copyright_xml – notice: 2019 The Author(s)
– notice: Copyright © 2019 The Author(s). Published by Elsevier B.V. All rights reserved.
DBID 6I.
AAFTH
AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7X8
DOI 10.1016/j.bbamem.2019.183154
DatabaseName ScienceDirect Open Access Titles
Elsevier:ScienceDirect:Open Access
CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
MEDLINE - Academic
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
MEDLINE - Academic
DatabaseTitleList
MEDLINE - Academic
MEDLINE
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: 7X8
  name: MEDLINE - Academic
  url: https://search.proquest.com/medline
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Chemistry
Biology
EISSN 1879-2642
ExternalDocumentID 31866287
10_1016_j_bbamem_2019_183154
S0005273619303025
Genre Research Support, Non-U.S. Gov't
Journal Article
Review
GroupedDBID ---
--K
--M
.~1
0R~
1B1
1RT
1~.
1~5
23N
4.4
457
4G.
5GY
5RE
5VS
6I.
6J9
7-5
71M
8P~
9JM
AABNK
AACTN
AAEDT
AAEDW
AAFTH
AAIAV
AAIKJ
AAKOC
AALRI
AAOAW
AAQFI
AAXUO
ABGSF
ABMAC
ABUDA
ABVKL
ABYKQ
ACDAQ
ACIUM
ACRLP
ADBBV
ADEZE
ADUVX
AEBSH
AEHWI
AEKER
AEXQZ
AFKWA
AFTJW
AFXIZ
AGUBO
AGYEJ
AHHHB
AIEXJ
AIKHN
AITUG
AJOXV
ALMA_UNASSIGNED_HOLDINGS
AMFUW
AMRAJ
AXJTR
BKOJK
BLXMC
CS3
EBS
EFJIC
EFLBG
EO8
EO9
EP2
EP3
FDB
FIRID
FNPLU
FYGXN
G-Q
GBLVA
IHE
IXB
J1W
KOM
LX3
M41
MO0
N9A
O-L
O9-
OAUVE
OK1
OZT
P-8
P-9
PC.
Q38
ROL
RPZ
SCC
SDF
SDG
SDP
SES
SSU
SSZ
T5K
WH7
XPP
~G-
3O-
53G
9DU
AAQXK
AATTM
AAXKI
AAYWO
AAYXX
ABDPE
ABEFU
ABFNM
ABWVN
ABXDB
ACLOT
ACRPL
ADMUD
ADNMO
ADVLN
AEIPS
AFJKZ
AGHFR
AGQPQ
AIIUN
ANKPU
ASPBG
AVWKF
AZFZN
CITATION
EFKBS
EJD
FEDTE
FGOYB
G-2
HLW
HVGLF
HZ~
R2-
RSU
SBG
SEW
WUQ
~HD
0SF
CGR
CUY
CVF
ECM
EIF
NPM
7X8
ID FETCH-LOGICAL-c474t-cb896ca1d58ff50d2ca414ac99226399d2ef3a8dafcff971cbb8b68ed70f74183
ISICitedReferencesCount 83
ISICitedReferencesURI http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000571408600002&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN 0005-2736
1879-2642
IngestDate Sat Sep 27 18:03:15 EDT 2025
Wed Feb 19 02:29:56 EST 2025
Sat Nov 29 06:58:37 EST 2025
Tue Nov 18 21:56:19 EST 2025
Fri Feb 23 02:46:17 EST 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 12
Keywords MATE superfamily
Multi-drug resistance
Transporter
Structural biology
Crystal structure
Language English
License This is an open access article under the CC BY-NC-ND license.
Copyright © 2019 The Author(s). Published by Elsevier B.V. All rights reserved.
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-c474t-cb896ca1d58ff50d2ca414ac99226399d2ef3a8dafcff971cbb8b68ed70f74183
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
ObjectType-Review-3
content type line 23
OpenAccessLink https://dx.doi.org/10.1016/j.bbamem.2019.183154
PMID 31866287
PQID 2330059551
PQPubID 23479
ParticipantIDs proquest_miscellaneous_2330059551
pubmed_primary_31866287
crossref_citationtrail_10_1016_j_bbamem_2019_183154
crossref_primary_10_1016_j_bbamem_2019_183154
elsevier_sciencedirect_doi_10_1016_j_bbamem_2019_183154
PublicationCentury 2000
PublicationDate 2020-12-01
2020-12-00
20201201
PublicationDateYYYYMMDD 2020-12-01
PublicationDate_xml – month: 12
  year: 2020
  text: 2020-12-01
  day: 01
PublicationDecade 2020
PublicationPlace Netherlands
PublicationPlace_xml – name: Netherlands
PublicationTitle Biochimica et biophysica acta. Biomembranes
PublicationTitleAlternate Biochim Biophys Acta Biomembr
PublicationYear 2020
Publisher Elsevier B.V
Publisher_xml – name: Elsevier B.V
References Durrett, Gassmann, Rogers (bb0110) 2007; 144
Yan (bb0140) 2015; 44
Thompson, Wilkins, Demidchik, Davies, Glover (bb0100) 2010; 61
Morita, Kodama, Shiota, Mine, Kataoka, Mizushima, Tsuchiya (bb0015) 1998; 42
Eisinger, Nie, Dörrbaum, Langer, Michel (bb0170) 2018; 430
Otsuka, Yasuda, Morita, Otsuka, Tsuchiya, Omote, Moriyama (bb0160) 2005; 187
Braibant, Guilloteau, Zygmunt (bb0035) 2002; 46
Brown, Paulsen, Skurray (bb0125) 1999; 31
Takanashi, Shitan, Yazaki (bb0090) 2014; 31
Li, He, Pandey, Tsuchiya, Luan (bb0265) 2002; 277
Nishima, Mizukami, Tanaka, Ishitani, Nureki, Sugita (bb0240) 2016; 110
Kuroda, Tsuchiya (bb0045) 2009; 1794
Kaatz, McAleese, Seo (bb0050) 2005; 49
Morita, Kataoka, Shiota, Mizushima, Tsuchiya (bb0020) 2000; 182
Omote, Hiasa, Matsumoto, Otsuka, Moriyama (bb0130) 2006; 27
Drew, Boudker (bb0195) 2016; 85
Long, Rouquette-Loughlin, Shafer, Yu (bb0150) 2008; 52
Huda, Morita, Kuroda, Mizushima, Tsuchiya (bb0040) 2001; 203
Tanaka, Iwaki, Tsukazaki (bb0255) 2017; 25
Masuda, Terada, Yonezawa, Tanihara, Kishimoto, Katsura, Ogawa, Inui (bb0070) 2006; 17
Jin, Nair, van Veen (bb0175) 2014; 289
Chen, Morita, Huda, Kuroda, Mizushima, Tsuchiya (bb0205) 2002; 184
Lu, Radchenko, Symersky, Nie, Guo (bb0220) 2013; 20
Hipolito, Tanaka, Katoh, Nureki, Suga (bb0235) 2013; 18
Ficici, Zhou, Castellano, Faraldo-Gómez (bb0245) 2018; 115
Du, van Veen, Murakami, Pos, Luisi (bb0005) 2015; 33
Begum, Rahman, Ogawa, Mizushima, Kuroda, Tsuchiya (bb0200) 2005; 49
Vanni, Campomanes, Marcia, Rothlisberger (bb0185) 2012; 51
Lu, Symersky, Radchenko, Koide, Guo, Nie, Koide (bb0155) 2013; 110
Ito, Kusuhara, Yokochi, Toyoshima, Inoue, Yuasa, Sugiyama (bb0080) 2012; 340
Miyauchi, Moriyama, Kusakizako, Kumazaki, Nakane, Yamashita, Hirata, Dohmae, Nishizawa, Ito, Miyaji, Moriyama, Ishitani, Nureki (bb0135) 2017; 8
Yokoo, Yonezawa, Masuda, Fukatsu, Katsura, Inui (bb0075) 2007; 74
Wagner, Hu, Wang (bb0085) 2016; 111
Otsuka, Matsumoto, Morimoto, Arioka, Omote, Moriyama (bb0060) 2005; 102
Tanaka, Hipolito, Maturana, Ito, Kuroda, Higuchi, Katoh, Kato, Hattori, Kumazaki, Tsukazaki, Ishitani, Suga, Nureki (bb0210) 2013; 496
Matsumoto, Kanamoto, Otsuka, Omote, Moriyama (bb0250) 2008; 294
Morita, Shitan, Sawada, Van Montagu, Inzé, Rischer, Goossens, Oksman-Caldentey, Moriyama, Yazaki (bb0095) 2009; 106
Radchenko, Symersky, Nie, Lu (bb0190) 2015; 6
He, Kuroda, Mima, Morita, Mizushima, Tsuchiya (bb0025) 2004; 186
He, Szewczyk, Karyakin, Evin, Hong, Zhang, Chang (bb0145) 2010; 467
McAleese, Petersen, Ruzin, Dunman, Murphy, Projan, Bradford (bb0055) 2005; 49
Tanihara, Masuda, Sato, Katsura, Ogawa, Inui (bb0065) 2007; 74
Shoji, Inai, Yazaki, Sato, Takase, Shitan, Yazaki, Goto, Toyooka, Matsuoka, Hashimoto (bb0260) 2009; 149
Nie, Grell, Malviya, Xie, Wang, Michel (bb0165) 2016; 291
Liu, Magalhaes, Shaff, Kochian (bb0115) 2009; 57
Kusakizako, Claxton, Tanaka, Maturana, Kuroda, Ishitani, Mchaourab, Nureki (bb0225) 2019; 27
Su, Chen, Mizushima, Kuroda, Tsuchiya (bb0030) 2005; 49
Huda, Chen, Morita, Kuroda, Mizushima, Tsuchiya (bb0215) 2003; 47
Marinova, Pourcel, Weder, Schwarz, Barron, Routaboul, Debeaujon, Kleina (bb0105) 2007; 19
Zakrzewska, Mehdipour, Malviya, Nonaka, Koepke, Muenke, Hausner, Hummer, Safarian, Michel (bb0230) 2019; 116
Hassan, Liu, Elbourne, Ahmad, Sharples, Naidu, Chan, Li, Harborne, Pokhrel, Postis, Goldman, Henderson, Paulsen (bb0010) 2018; 169
Claxton, Jagessar, Steed, Stein, Mchaourab (bb0180) 2018; 115
Pineau, Loubet, Lefoulon, Chalies, Fizames, Lacombe, Ferrand, Loudet, Berthomieu, Richard (bb0120) 2012; 8
Yan (10.1016/j.bbamem.2019.183154_bb0140) 2015; 44
Pineau (10.1016/j.bbamem.2019.183154_bb0120) 2012; 8
Kaatz (10.1016/j.bbamem.2019.183154_bb0050) 2005; 49
Otsuka (10.1016/j.bbamem.2019.183154_bb0160) 2005; 187
Begum (10.1016/j.bbamem.2019.183154_bb0200) 2005; 49
He (10.1016/j.bbamem.2019.183154_bb0145) 2010; 467
Shoji (10.1016/j.bbamem.2019.183154_bb0260) 2009; 149
Vanni (10.1016/j.bbamem.2019.183154_bb0185) 2012; 51
Claxton (10.1016/j.bbamem.2019.183154_bb0180) 2018; 115
Ito (10.1016/j.bbamem.2019.183154_bb0080) 2012; 340
Huda (10.1016/j.bbamem.2019.183154_bb0040) 2001; 203
Tanaka (10.1016/j.bbamem.2019.183154_bb0255) 2017; 25
Huda (10.1016/j.bbamem.2019.183154_bb0215) 2003; 47
Braibant (10.1016/j.bbamem.2019.183154_bb0035) 2002; 46
Jin (10.1016/j.bbamem.2019.183154_bb0175) 2014; 289
Li (10.1016/j.bbamem.2019.183154_bb0265) 2002; 277
Marinova (10.1016/j.bbamem.2019.183154_bb0105) 2007; 19
Lu (10.1016/j.bbamem.2019.183154_bb0220) 2013; 20
Omote (10.1016/j.bbamem.2019.183154_bb0130) 2006; 27
Hipolito (10.1016/j.bbamem.2019.183154_bb0235) 2013; 18
Lu (10.1016/j.bbamem.2019.183154_bb0155) 2013; 110
Nie (10.1016/j.bbamem.2019.183154_bb0165) 2016; 291
Drew (10.1016/j.bbamem.2019.183154_bb0195) 2016; 85
Durrett (10.1016/j.bbamem.2019.183154_bb0110) 2007; 144
Wagner (10.1016/j.bbamem.2019.183154_bb0085) 2016; 111
Du (10.1016/j.bbamem.2019.183154_bb0005) 2015; 33
Morita (10.1016/j.bbamem.2019.183154_bb0015) 1998; 42
Masuda (10.1016/j.bbamem.2019.183154_bb0070) 2006; 17
Zakrzewska (10.1016/j.bbamem.2019.183154_bb0230) 2019; 116
Matsumoto (10.1016/j.bbamem.2019.183154_bb0250) 2008; 294
Otsuka (10.1016/j.bbamem.2019.183154_bb0060) 2005; 102
Radchenko (10.1016/j.bbamem.2019.183154_bb0190) 2015; 6
Morita (10.1016/j.bbamem.2019.183154_bb0020) 2000; 182
Chen (10.1016/j.bbamem.2019.183154_bb0205) 2002; 184
Eisinger (10.1016/j.bbamem.2019.183154_bb0170) 2018; 430
Ficici (10.1016/j.bbamem.2019.183154_bb0245) 2018; 115
Tanihara (10.1016/j.bbamem.2019.183154_bb0065) 2007; 74
Kusakizako (10.1016/j.bbamem.2019.183154_bb0225) 2019; 27
Su (10.1016/j.bbamem.2019.183154_bb0030) 2005; 49
Tanaka (10.1016/j.bbamem.2019.183154_bb0210) 2013; 496
Brown (10.1016/j.bbamem.2019.183154_bb0125) 1999; 31
McAleese (10.1016/j.bbamem.2019.183154_bb0055) 2005; 49
Miyauchi (10.1016/j.bbamem.2019.183154_bb0135) 2017; 8
Thompson (10.1016/j.bbamem.2019.183154_bb0100) 2010; 61
Hassan (10.1016/j.bbamem.2019.183154_bb0010) 2018; 169
Yokoo (10.1016/j.bbamem.2019.183154_bb0075) 2007; 74
Takanashi (10.1016/j.bbamem.2019.183154_bb0090) 2014; 31
Kuroda (10.1016/j.bbamem.2019.183154_bb0045) 2009; 1794
Liu (10.1016/j.bbamem.2019.183154_bb0115) 2009; 57
Morita (10.1016/j.bbamem.2019.183154_bb0095) 2009; 106
Nishima (10.1016/j.bbamem.2019.183154_bb0240) 2016; 110
He (10.1016/j.bbamem.2019.183154_bb0025) 2004; 186
Long (10.1016/j.bbamem.2019.183154_bb0150) 2008; 52
References_xml – volume: 294
  start-page: C1074
  year: 2008
  end-page: C1078
  ident: bb0250
  article-title: Role of glutamate residues in substrate recognition by human MATE1 polyspecific H
  publication-title: Am. J. Physiol. Cell Physiol.
– volume: 49
  start-page: 4362
  year: 2005
  end-page: 4364
  ident: bb0030
  article-title: AbeM, an H
  publication-title: Antimicrob. Agents Chemother.
– volume: 149
  start-page: 708
  year: 2009
  end-page: 718
  ident: bb0260
  article-title: Multidrug and toxic compound extrusion-type transporters implicated in vacuolar sequestration of nicotine in tobacco roots
  publication-title: Plant Physiol.
– volume: 277
  start-page: 5360
  year: 2002
  end-page: 5368
  ident: bb0265
  article-title: Functional cloning and characterization of a plant efflux carrier for multidrug and heavy metal detoxification
  publication-title: J. Biol. Chem.
– volume: 8
  year: 2017
  ident: bb0135
  article-title: Structural basis for xenobiotic extrusion by eukaryotic MATE transporter
  publication-title: Nat. Commun.
– volume: 6
  start-page: 7995
  year: 2015
  ident: bb0190
  article-title: Structural basis for the blockade of MATE multidrug efflux pumps
  publication-title: Nat. Commun.
– volume: 169
  start-page: 450
  year: 2018
  end-page: 454
  ident: bb0010
  article-title: Pacing across the membrane: the novel PACE family of efflux pumps is widespread in Gram-negative pathogens
  publication-title: Res. Microbiol.
– volume: 42
  start-page: 1778
  year: 1998
  end-page: 1782
  ident: bb0015
  article-title: NorM, a putative multidrug efflux protein, of
  publication-title: Antimicrob. Agents Chemother.
– volume: 182
  start-page: 6694
  year: 2000
  end-page: 6697
  ident: bb0020
  article-title: NorM of
  publication-title: J. Bacteriol.
– volume: 115
  start-page: E6172
  year: 2018
  end-page: E6181
  ident: bb0245
  article-title: Broadly conserved Na
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 110
  start-page: 2099
  year: 2013
  end-page: 2104
  ident: bb0155
  article-title: Structures of a Na
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 291
  start-page: 15503
  year: 2016
  end-page: 15514
  ident: bb0165
  article-title: Identification of the high-affinity substrate-binding site of the multidrug and toxic compound extrusion (MATE) family transporter from
  publication-title: J. Biol. Chem.
– volume: 57
  start-page: 389
  year: 2009
  end-page: 399
  ident: bb0115
  article-title: Aluminum-activated citrate and malate transporters from the MATE and ALMT families function independently to confer Arabidopsis aluminum tolerance
  publication-title: Plant J.
– volume: 31
  start-page: 394
  year: 1999
  end-page: 395
  ident: bb0125
  article-title: The multidrug efflux protein NorM is a prototype of a new family of transporters
  publication-title: Mol. Microbiol.
– volume: 102
  start-page: 17923
  year: 2005
  end-page: 17928
  ident: bb0060
  article-title: A human transporter protein that mediates the final excretion step for toxic organic cations
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 111
  start-page: 237
  year: 2016
  end-page: 246
  ident: bb0085
  article-title: Polyspecific organic cation transporters and their impact on drug intracellular levels and pharmacodynamics
  publication-title: Pharmacol. Res.
– volume: 85
  start-page: 543
  year: 2016
  end-page: 572
  ident: bb0195
  article-title: Shared molecular mechanisms of membrane transporters
  publication-title: Annu. Rev. Biochem.
– volume: 115
  start-page: E6182
  year: 2018
  end-page: E6190
  ident: bb0180
  article-title: Sodium and proton coupling in the conformational cycle of a MATE antiporter from
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 49
  start-page: 949
  year: 2005
  end-page: 957
  ident: bb0200
  article-title: Gene cloning and characterization of four MATE family multidrug efflux pumps from
  publication-title: Microbiol. Immunol.
– volume: 74
  start-page: 477
  year: 2007
  end-page: 487
  ident: bb0075
  article-title: Differential contribution of organic cation transporters, OCT2 and MATE1, in platinum agent-induced nephrotoxicity
  publication-title: Biochem. Pharmacol.
– volume: 289
  start-page: 14624
  year: 2014
  end-page: 14632
  ident: bb0175
  article-title: Multidrug transport protein NorM from
  publication-title: J. Biol. Chem.
– volume: 106
  start-page: 2447
  year: 2009
  end-page: 2452
  ident: bb0095
  article-title: Vacuolar transport of nicotine is mediated by a multidrug and toxic compound extrusion (MATE) transporter in
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 184
  start-page: 572
  year: 2002
  end-page: 576
  ident: bb0205
  article-title: VmrA, a member of a novel class of Na
  publication-title: J. Bacteriol.
– volume: 19
  start-page: 2023
  year: 2007
  end-page: 2038
  ident: bb0105
  article-title: The
  publication-title: Plant Cell
– volume: 33
  start-page: 76
  year: 2015
  end-page: 91
  ident: bb0005
  article-title: Structure, mechanism and cooperation of bacterial multidrug transporters
  publication-title: Curr. Opin. Struct. Biol.
– volume: 61
  start-page: 439
  year: 2010
  end-page: 451
  ident: bb0100
  article-title: An
  publication-title: J. Exp. Bot.
– volume: 203
  start-page: 235
  year: 2001
  end-page: 239
  ident: bb0040
  article-title: Na
  publication-title: FEMS Microbiol. Lett.
– volume: 467
  start-page: 991
  year: 2010
  end-page: 994
  ident: bb0145
  article-title: Structure of a cation-bound multidrug and toxic compound extrusion transporter
  publication-title: Nature.
– volume: 44
  start-page: 257
  year: 2015
  end-page: 283
  ident: bb0140
  article-title: Structural biology of the major facilitator superfamily transporters
  publication-title: Annu. Rev. Biophys.
– volume: 46
  start-page: 3050
  year: 2002
  end-page: 3053
  ident: bb0035
  article-title: Functional characterization of
  publication-title: Antimicrob. Agents Chemother.
– volume: 8
  year: 2012
  ident: bb0120
  article-title: Natural variation at the FRD3 MATE transporter locus reveals cross-talk between Fe homeostasis and Zn tolerance in
  publication-title: PLoS Genet.
– volume: 430
  start-page: 1311
  year: 2018
  end-page: 1323
  ident: bb0170
  article-title: The xenobiotic extrusion mechanism of the MATE transporter NorM_PS from
  publication-title: J. Mol. Biol.
– volume: 116
  start-page: 12275
  year: 2019
  end-page: 12284
  ident: bb0230
  article-title: Inward-facing conformation of a multidrug resistance MATE family transporter
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
– volume: 496
  start-page: 247
  year: 2013
  end-page: 251
  ident: bb0210
  article-title: Structural basis for the drug extrusion mechanism by a MATE multidrug transporter
  publication-title: Nature.
– volume: 49
  start-page: 1865
  year: 2005
  end-page: 1871
  ident: bb0055
  article-title: A novel MATE family efflux pump contributes to the reduced susceptibility of laboratory-derived
  publication-title: Antimicrob. Agents Chemother.
– volume: 49
  start-page: 1857
  year: 2005
  end-page: 1864
  ident: bb0050
  article-title: Multidrug resistance in
  publication-title: Antimicrobiol Agents and Chmotherapy.
– volume: 25
  start-page: 1455
  year: 2017
  end-page: 1460.e2
  ident: bb0255
  article-title: Crystal structure of a plant multidrug and toxic compound extrusion family protein
  publication-title: Structure
– volume: 1794
  start-page: 763
  year: 2009
  end-page: 768
  ident: bb0045
  article-title: Multidrug efflux transporters in the MATE family
  publication-title: Biochimica et Biophysica Acta - Proteins and Proteomics.
– volume: 20
  start-page: 1310
  year: 2013
  end-page: 1317
  ident: bb0220
  article-title: Structural insights into H
  publication-title: Nat. Struct. Mol. Biol.
– volume: 18
  start-page: 10514
  year: 2013
  end-page: 10530
  ident: bb0235
  article-title: A macrocyclic peptide that serves as a cocrystallization ligand and inhibits the function of a MATE family transporter
  publication-title: Molecules.
– volume: 144
  start-page: 197
  year: 2007
  end-page: 205
  ident: bb0110
  article-title: The FRD3-mediated efflux of citrate into the root vasculature is necessary for efficient iron translocation
  publication-title: Plant Physiol.
– volume: 47
  start-page: 419
  year: 2003
  end-page: 427
  ident: bb0215
  article-title: Gene cloning and characterization of VcrM, a Na
  publication-title: Microbiol. Immunol.
– volume: 74
  start-page: 359
  year: 2007
  end-page: 371
  ident: bb0065
  article-title: Substrate specificity of MATE1 and MATE2-K, human multidrug and toxin extrusions/H
  publication-title: Biochem. Pharmacol.
– volume: 17
  start-page: 2127
  year: 2006
  end-page: 2135
  ident: bb0070
  article-title: Identification and functional characterization of a new human kidney-specific H
  publication-title: J. Am. Soc. Nephrol.
– volume: 186
  start-page: 262
  year: 2004
  end-page: 265
  ident: bb0025
  article-title: An H
  publication-title: J. Bacteriol.
– volume: 110
  start-page: 1346
  year: 2016
  end-page: 1354
  ident: bb0240
  article-title: Mechanisms for two-step proton transfer reactions in the outward-facing form of MATE transporter
  publication-title: Biophys. J.
– volume: 340
  start-page: 393
  year: 2012
  end-page: 403
  ident: bb0080
  article-title: Competitive inhibition of the luminal efflux by multidrug and toxin extrusions, but not basolateral uptake by organic cation transporter 2, is the likely mechanism underlying the pharmacokinetic drug-drug interactions caused by cimetidine in the kidney
  publication-title: J. Pharmacol. Exp. Ther.
– volume: 27
  start-page: 587
  year: 2006
  end-page: 593
  ident: bb0130
  article-title: The MATE proteins as fundamental transporters of metabolic and xenobiotic organic cations
  publication-title: Trends Pharmacol. Sci.
– volume: 51
  start-page: 1281
  year: 2012
  end-page: 1287
  ident: bb0185
  article-title: Ion binding and internal hydration in the multidrug resistance secondary active transporter NorM investigated by molecular dynamics simulations
  publication-title: Biochemistry.
– volume: 187
  start-page: 1552
  year: 2005
  end-page: 1558
  ident: bb0160
  article-title: Identification of essential amino acid residues of the NorM Na
  publication-title: J. Bacteriol.
– volume: 27
  start-page: 293
  year: 2019
  end-page: 301.e3
  ident: bb0225
  article-title: Structural basis of H
  publication-title: Structure
– volume: 31
  start-page: 417
  year: 2014
  end-page: 430
  ident: bb0090
  article-title: The multidrug and toxic compound extrusion (MATE) family in plants
  publication-title: Plant Biotechnology.
– volume: 52
  start-page: 3052
  year: 2008
  end-page: 3060
  ident: bb0150
  article-title: Functional cloning and characterization of the multidrug efflux pumps NorM from
  publication-title: Antimicrob. Agents Chemother.
– volume: 186
  start-page: 262
  year: 2004
  ident: 10.1016/j.bbamem.2019.183154_bb0025
  article-title: An H+-coupled multidrug efflux pump, PmpM, a member of the MATE family of transporters, from Pseudomonas aeruginosa
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.186.1.262-265.2004
– volume: 27
  start-page: 587
  year: 2006
  ident: 10.1016/j.bbamem.2019.183154_bb0130
  article-title: The MATE proteins as fundamental transporters of metabolic and xenobiotic organic cations
  publication-title: Trends Pharmacol. Sci.
  doi: 10.1016/j.tips.2006.09.001
– volume: 430
  start-page: 1311
  year: 2018
  ident: 10.1016/j.bbamem.2019.183154_bb0170
  article-title: The xenobiotic extrusion mechanism of the MATE transporter NorM_PS from Pseudomonas stutzeri
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2018.03.012
– volume: 31
  start-page: 394
  year: 1999
  ident: 10.1016/j.bbamem.2019.183154_bb0125
  article-title: The multidrug efflux protein NorM is a prototype of a new family of transporters
  publication-title: Mol. Microbiol.
  doi: 10.1046/j.1365-2958.1999.01162.x
– volume: 46
  start-page: 3050
  year: 2002
  ident: 10.1016/j.bbamem.2019.183154_bb0035
  article-title: Functional characterization of Brucella melitensis NorMI, an efflux pump belonging to the multidrug and toxic compound extrusion family
  publication-title: Antimicrob. Agents Chemother.
  doi: 10.1128/AAC.46.9.3050-3053.2002
– volume: 1794
  start-page: 763
  year: 2009
  ident: 10.1016/j.bbamem.2019.183154_bb0045
  article-title: Multidrug efflux transporters in the MATE family
  publication-title: Biochimica et Biophysica Acta - Proteins and Proteomics.
  doi: 10.1016/j.bbapap.2008.11.012
– volume: 52
  start-page: 3052
  year: 2008
  ident: 10.1016/j.bbamem.2019.183154_bb0150
  article-title: Functional cloning and characterization of the multidrug efflux pumps NorM from Neisseria gonorrhoeae and YdhE from Escherichia coli
  publication-title: Antimicrob. Agents Chemother.
  doi: 10.1128/AAC.00475-08
– volume: 18
  start-page: 10514
  year: 2013
  ident: 10.1016/j.bbamem.2019.183154_bb0235
  article-title: A macrocyclic peptide that serves as a cocrystallization ligand and inhibits the function of a MATE family transporter
  publication-title: Molecules.
  doi: 10.3390/molecules180910514
– volume: 340
  start-page: 393
  year: 2012
  ident: 10.1016/j.bbamem.2019.183154_bb0080
  article-title: Competitive inhibition of the luminal efflux by multidrug and toxin extrusions, but not basolateral uptake by organic cation transporter 2, is the likely mechanism underlying the pharmacokinetic drug-drug interactions caused by cimetidine in the kidney
  publication-title: J. Pharmacol. Exp. Ther.
  doi: 10.1124/jpet.111.184986
– volume: 33
  start-page: 76
  year: 2015
  ident: 10.1016/j.bbamem.2019.183154_bb0005
  article-title: Structure, mechanism and cooperation of bacterial multidrug transporters
  publication-title: Curr. Opin. Struct. Biol.
  doi: 10.1016/j.sbi.2015.07.015
– volume: 110
  start-page: 1346
  year: 2016
  ident: 10.1016/j.bbamem.2019.183154_bb0240
  article-title: Mechanisms for two-step proton transfer reactions in the outward-facing form of MATE transporter
  publication-title: Biophys. J.
  doi: 10.1016/j.bpj.2016.01.027
– volume: 187
  start-page: 1552
  year: 2005
  ident: 10.1016/j.bbamem.2019.183154_bb0160
  article-title: Identification of essential amino acid residues of the NorM Na+/multidrug antiporter in Vibrio parahaemolyticus
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.187.5.1552-1558.2005
– volume: 184
  start-page: 572
  year: 2002
  ident: 10.1016/j.bbamem.2019.183154_bb0205
  article-title: VmrA, a member of a novel class of Na+-coupled multidrug efflux pumps from Vibrio parahaemolyticus
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.184.2.572-576.2002
– volume: 203
  start-page: 235
  year: 2001
  ident: 10.1016/j.bbamem.2019.183154_bb0040
  article-title: Na+-driven multidrug efflux pump VcmA from Vibrio cholerae non-O1, a non-halophilic bacterium
  publication-title: FEMS Microbiol. Lett.
  doi: 10.1111/j.1574-6968.2001.tb10847.x
– volume: 8
  year: 2012
  ident: 10.1016/j.bbamem.2019.183154_bb0120
  article-title: Natural variation at the FRD3 MATE transporter locus reveals cross-talk between Fe homeostasis and Zn tolerance in Arabidopsis thaliana
  publication-title: PLoS Genet.
  doi: 10.1371/journal.pgen.1003120
– volume: 85
  start-page: 543
  year: 2016
  ident: 10.1016/j.bbamem.2019.183154_bb0195
  article-title: Shared molecular mechanisms of membrane transporters
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev-biochem-060815-014520
– volume: 294
  start-page: C1074
  year: 2008
  ident: 10.1016/j.bbamem.2019.183154_bb0250
  article-title: Role of glutamate residues in substrate recognition by human MATE1 polyspecific H+/organic cation exporter
  publication-title: Am. J. Physiol. Cell Physiol.
  doi: 10.1152/ajpcell.00504.2007
– volume: 31
  start-page: 417
  year: 2014
  ident: 10.1016/j.bbamem.2019.183154_bb0090
  article-title: The multidrug and toxic compound extrusion (MATE) family in plants
  publication-title: Plant Biotechnology.
  doi: 10.5511/plantbiotechnology.14.0904a
– volume: 8
  year: 2017
  ident: 10.1016/j.bbamem.2019.183154_bb0135
  article-title: Structural basis for xenobiotic extrusion by eukaryotic MATE transporter
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-017-01541-0
– volume: 49
  start-page: 949
  year: 2005
  ident: 10.1016/j.bbamem.2019.183154_bb0200
  article-title: Gene cloning and characterization of four MATE family multidrug efflux pumps from Vibrio cholerae non-O1
  publication-title: Microbiol. Immunol.
  doi: 10.1111/j.1348-0421.2005.tb03690.x
– volume: 467
  start-page: 991
  year: 2010
  ident: 10.1016/j.bbamem.2019.183154_bb0145
  article-title: Structure of a cation-bound multidrug and toxic compound extrusion transporter
  publication-title: Nature.
  doi: 10.1038/nature09408
– volume: 49
  start-page: 1865
  year: 2005
  ident: 10.1016/j.bbamem.2019.183154_bb0055
  article-title: A novel MATE family efflux pump contributes to the reduced susceptibility of laboratory-derived Staphylococcus aureus mutants to tigecycline
  publication-title: Antimicrob. Agents Chemother.
  doi: 10.1128/AAC.49.5.1865-1871.2005
– volume: 61
  start-page: 439
  year: 2010
  ident: 10.1016/j.bbamem.2019.183154_bb0100
  article-title: An Arabidopsis flavonoid transporter is required for anther dehiscence and pollen development
  publication-title: J. Exp. Bot.
  doi: 10.1093/jxb/erp312
– volume: 291
  start-page: 15503
  year: 2016
  ident: 10.1016/j.bbamem.2019.183154_bb0165
  article-title: Identification of the high-affinity substrate-binding site of the multidrug and toxic compound extrusion (MATE) family transporter from Pseudomonas stutzeri
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M116.728618
– volume: 49
  start-page: 4362
  year: 2005
  ident: 10.1016/j.bbamem.2019.183154_bb0030
  article-title: AbeM, an H+-coupled Acinetobacter baumannii multidrug efflux pump belonging to the MATE family of transporters
  publication-title: Antimicrob. Agents Chemother.
  doi: 10.1128/AAC.49.10.4362-4364.2005
– volume: 289
  start-page: 14624
  year: 2014
  ident: 10.1016/j.bbamem.2019.183154_bb0175
  article-title: Multidrug transport protein NorM from Vibrio cholerae simultaneously couples to sodium- and proton-motive force
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M113.546770
– volume: 74
  start-page: 477
  year: 2007
  ident: 10.1016/j.bbamem.2019.183154_bb0075
  article-title: Differential contribution of organic cation transporters, OCT2 and MATE1, in platinum agent-induced nephrotoxicity
  publication-title: Biochem. Pharmacol.
  doi: 10.1016/j.bcp.2007.03.004
– volume: 144
  start-page: 197
  year: 2007
  ident: 10.1016/j.bbamem.2019.183154_bb0110
  article-title: The FRD3-mediated efflux of citrate into the root vasculature is necessary for efficient iron translocation
  publication-title: Plant Physiol.
  doi: 10.1104/pp.107.097162
– volume: 27
  start-page: 293
  year: 2019
  ident: 10.1016/j.bbamem.2019.183154_bb0225
  article-title: Structural basis of H+-dependent conformational change in a bacterial MATE transporter
  publication-title: Structure
  doi: 10.1016/j.str.2018.10.004
– volume: 102
  start-page: 17923
  year: 2005
  ident: 10.1016/j.bbamem.2019.183154_bb0060
  article-title: A human transporter protein that mediates the final excretion step for toxic organic cations
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0506483102
– volume: 17
  start-page: 2127
  year: 2006
  ident: 10.1016/j.bbamem.2019.183154_bb0070
  article-title: Identification and functional characterization of a new human kidney-specific H+/organic cation antiporter, kidney-specific multidrug and toxin extrusion 2
  publication-title: J. Am. Soc. Nephrol.
  doi: 10.1681/ASN.2006030205
– volume: 169
  start-page: 450
  year: 2018
  ident: 10.1016/j.bbamem.2019.183154_bb0010
  article-title: Pacing across the membrane: the novel PACE family of efflux pumps is widespread in Gram-negative pathogens
  publication-title: Res. Microbiol.
  doi: 10.1016/j.resmic.2018.01.001
– volume: 42
  start-page: 1778
  year: 1998
  ident: 10.1016/j.bbamem.2019.183154_bb0015
  article-title: NorM, a putative multidrug efflux protein, of Vibrio parahaemolyticus and its homolog in Escherichia coli
  publication-title: Antimicrob. Agents Chemother.
  doi: 10.1128/AAC.42.7.1778
– volume: 57
  start-page: 389
  year: 2009
  ident: 10.1016/j.bbamem.2019.183154_bb0115
  article-title: Aluminum-activated citrate and malate transporters from the MATE and ALMT families function independently to confer Arabidopsis aluminum tolerance
  publication-title: Plant J.
  doi: 10.1111/j.1365-313X.2008.03696.x
– volume: 25
  start-page: 1455
  year: 2017
  ident: 10.1016/j.bbamem.2019.183154_bb0255
  article-title: Crystal structure of a plant multidrug and toxic compound extrusion family protein
  publication-title: Structure
  doi: 10.1016/j.str.2017.07.009
– volume: 6
  start-page: 7995
  year: 2015
  ident: 10.1016/j.bbamem.2019.183154_bb0190
  article-title: Structural basis for the blockade of MATE multidrug efflux pumps
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms8995
– volume: 182
  start-page: 6694
  year: 2000
  ident: 10.1016/j.bbamem.2019.183154_bb0020
  article-title: NorM of Vibrio parahaemolyticus is an Na+-driven multidrug efflux pump
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.182.23.6694-6697.2000
– volume: 20
  start-page: 1310
  year: 2013
  ident: 10.1016/j.bbamem.2019.183154_bb0220
  article-title: Structural insights into H+-coupled multidrug extrusion by a MATE transporter
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.2687
– volume: 277
  start-page: 5360
  year: 2002
  ident: 10.1016/j.bbamem.2019.183154_bb0265
  article-title: Functional cloning and characterization of a plant efflux carrier for multidrug and heavy metal detoxification
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M108777200
– volume: 111
  start-page: 237
  year: 2016
  ident: 10.1016/j.bbamem.2019.183154_bb0085
  article-title: Polyspecific organic cation transporters and their impact on drug intracellular levels and pharmacodynamics
  publication-title: Pharmacol. Res.
  doi: 10.1016/j.phrs.2016.06.002
– volume: 106
  start-page: 2447
  year: 2009
  ident: 10.1016/j.bbamem.2019.183154_bb0095
  article-title: Vacuolar transport of nicotine is mediated by a multidrug and toxic compound extrusion (MATE) transporter in Nicotiana tabacum
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0812512106
– volume: 116
  start-page: 12275
  year: 2019
  ident: 10.1016/j.bbamem.2019.183154_bb0230
  article-title: Inward-facing conformation of a multidrug resistance MATE family transporter
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.1904210116
– volume: 47
  start-page: 419
  year: 2003
  ident: 10.1016/j.bbamem.2019.183154_bb0215
  article-title: Gene cloning and characterization of VcrM, a Na+-coupled multidrug efflux pump, from Vibrio cholerae non-O1
  publication-title: Microbiol. Immunol.
  doi: 10.1111/j.1348-0421.2003.tb03379.x
– volume: 115
  start-page: E6172
  year: 2018
  ident: 10.1016/j.bbamem.2019.183154_bb0245
  article-title: Broadly conserved Na+-binding site in the N-lobe of prokaryotic multidrug MATE transporters
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.1802080115
– volume: 496
  start-page: 247
  year: 2013
  ident: 10.1016/j.bbamem.2019.183154_bb0210
  article-title: Structural basis for the drug extrusion mechanism by a MATE multidrug transporter
  publication-title: Nature.
  doi: 10.1038/nature12014
– volume: 110
  start-page: 2099
  year: 2013
  ident: 10.1016/j.bbamem.2019.183154_bb0155
  article-title: Structures of a Na+-coupled, substrate-bound MATE multidrug transporter
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.1219901110
– volume: 51
  start-page: 1281
  year: 2012
  ident: 10.1016/j.bbamem.2019.183154_bb0185
  article-title: Ion binding and internal hydration in the multidrug resistance secondary active transporter NorM investigated by molecular dynamics simulations
  publication-title: Biochemistry.
  doi: 10.1021/bi2015184
– volume: 49
  start-page: 1857
  year: 2005
  ident: 10.1016/j.bbamem.2019.183154_bb0050
  article-title: Multidrug resistance in Staphylococcus aureus due to overexpression of a novel Multidrug and Toxin Extrusion (MATE) transport protein
  publication-title: Antimicrobiol Agents and Chmotherapy.
  doi: 10.1128/AAC.49.5.1857-1864.2005
– volume: 115
  start-page: E6182
  year: 2018
  ident: 10.1016/j.bbamem.2019.183154_bb0180
  article-title: Sodium and proton coupling in the conformational cycle of a MATE antiporter from Vibrio cholerae
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.1802417115
– volume: 149
  start-page: 708
  year: 2009
  ident: 10.1016/j.bbamem.2019.183154_bb0260
  article-title: Multidrug and toxic compound extrusion-type transporters implicated in vacuolar sequestration of nicotine in tobacco roots
  publication-title: Plant Physiol.
  doi: 10.1104/pp.108.132811
– volume: 74
  start-page: 359
  year: 2007
  ident: 10.1016/j.bbamem.2019.183154_bb0065
  article-title: Substrate specificity of MATE1 and MATE2-K, human multidrug and toxin extrusions/H+-organic cation antiporters
  publication-title: Biochem. Pharmacol.
  doi: 10.1016/j.bcp.2007.04.010
– volume: 19
  start-page: 2023
  year: 2007
  ident: 10.1016/j.bbamem.2019.183154_bb0105
  article-title: The Arabidopsis MATE transporter TT12 acts as a vacuolar flavonoid/H+-antiporter active in proanthocyanidin-accumulating cells of the seed coat
  publication-title: Plant Cell
  doi: 10.1105/tpc.106.046029
– volume: 44
  start-page: 257
  year: 2015
  ident: 10.1016/j.bbamem.2019.183154_bb0140
  article-title: Structural biology of the major facilitator superfamily transporters
  publication-title: Annu. Rev. Biophys.
  doi: 10.1146/annurev-biophys-060414-033901
SSID ssj0016425
Score 2.5961554
SecondaryResourceType review_article
Snippet Xenobiotic and metabolite extrusion is an important process for the proper functions of cells and their compartments, including acidic organelles. MATE...
SourceID proquest
pubmed
crossref
elsevier
SourceType Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 183154
SubjectTerms Archaea - metabolism
Archaeal Proteins - chemistry
Archaeal Proteins - classification
Archaeal Proteins - metabolism
ATP-Binding Cassette Transporters - chemistry
ATP-Binding Cassette Transporters - classification
ATP-Binding Cassette Transporters - metabolism
Crystal structure
Humans
MATE superfamily
Molecular Dynamics Simulation
Multi-drug resistance
Organic Cation Transport Proteins - chemistry
Organic Cation Transport Proteins - classification
Organic Cation Transport Proteins - metabolism
Plant Proteins - chemistry
Plant Proteins - classification
Plant Proteins - metabolism
Plants - metabolism
Protein Structure, Tertiary
Structural biology
Substrate Specificity
Transporter
Title Structural biology of the multidrug and toxic compound extrusion superfamily transporters
URI https://dx.doi.org/10.1016/j.bbamem.2019.183154
https://www.ncbi.nlm.nih.gov/pubmed/31866287
https://www.proquest.com/docview/2330059551
Volume 1862
WOSCitedRecordID wos000571408600002&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
journalDatabaseRights – providerCode: PRVESC
  databaseName: Elsevier SD Freedom Collection Journals 2021
  customDbUrl:
  eissn: 1879-2642
  dateEnd: 20210131
  omitProxy: false
  ssIdentifier: ssj0016425
  issn: 0005-2736
  databaseCode: AIEXJ
  dateStart: 19950126
  isFulltext: true
  titleUrlDefault: https://www.sciencedirect.com
  providerName: Elsevier
link http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1db9MwFLW6DQQvCAaD8jEZibcqVeMktfM4TUOAxEBQpPIUOY6tZV2TKh9Ty1_iT3Idx2lgGmMPvERVlLhOzsn19fX1uQi9cX0lKfepA94FcXyfTpw4DJVDifJoInjAiSk2QU9P2Xwefh4Mftq9MJcXNMvYeh2u_ivUcA7A1ltnbwF31yicgN8AOhwBdjj-E_BfG0XYRk3DKiy1eQBN8mBS1GZXYpWvU9GklOvKSiMw0kWtQ2ejsl7Jog18VJ32ebvqY9d_01ycpVpqYCQr_T8mQsK1Ngcf6wqXS7mEiXgme4tFJXirP_iiCc7OynrBy25M-JhuuC7L0oyEaZFXfCG3rD1LK1N6avRlU6dwWZF3Qey6kKby9qeSL-t-EIP0E0KsYdZb44wWytYwT0mfgqRnaMESuUZ9-soYYMIR5-M45vCoOnsvHG8v_11y-4-hsEtQtLlv55FpJdKtRKaVHbRHaBCCCd07en8y_9AtWsFUzhTMaJ_F7tRs0gmv9uY6T-i6mU7j8cweogftVAUfGYo9QgOZ7aO7pnjpZh_dO7a1Ah-j71vS4ZZ0OFcYSIc70mEgHW5Ihy3pcEc63CMd7pPuCfr29mR2_M5pi3Y4wqd-5YiYhVPB3SRgSgWThAjuuz4XWv9Ye8MJkcrjLOFKKBVSV8Qxi6dMJnSitJKSd4B2szyTzxCO1dSnMIOIkwScUBKwOA59pRLmMz4JeDBEnn2BkWgV7XVhlYvob_ANkdPdtTKKLjdcTy02UeuVGm8zAsLdcOdrC2UEeOiVOPjs8rqMiKerRIQwWxmipwbjri-elqAkjD6_ZT9foPvbL-sl2gX85Ct0R1xWaVkcoh06Z4ctY38BAyrLNA
linkProvider Elsevier
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Structural+biology+of+the+multidrug+and+toxic+compound+extrusion+superfamily+transporters&rft.jtitle=Biochimica+et+biophysica+acta.+Biomembranes&rft.au=Kusakizako%2C+Tsukasa&rft.au=Miyauchi%2C+Hirotake&rft.au=Ishitani%2C+Ryuichiro&rft.au=Nureki%2C+Osamu&rft.date=2020-12-01&rft.issn=0005-2736&rft.volume=1862&rft.issue=12&rft.spage=183154&rft_id=info:doi/10.1016%2Fj.bbamem.2019.183154&rft.externalDBID=n%2Fa&rft.externalDocID=10_1016_j_bbamem_2019_183154
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0005-2736&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0005-2736&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0005-2736&client=summon