Structural and mechanistic insights into fungal β-1,3-glucan synthase FKS1

The membrane-integrated synthase FKS is involved in the biosynthesis of β-1,3-glucan, the core component of the fungal cell wall 1 , 2 . FKS is the target of widely prescribed antifungal drugs, including echinocandin and ibrexafungerp 3 , 4 . Unfortunately, the mechanism of action of FKS remains eni...

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Published in:Nature (London) Vol. 616; no. 7955; pp. 190 - 198
Main Authors: Hu, Xinlin, Yang, Ping, Chai, Changdong, Liu, Jia, Sun, Huanhuan, Wu, Yanan, Zhang, Mingjie, Zhang, Min, Liu, Xiaotian, Yu, Hongjun
Format: Journal Article
Language:English
Published: London Nature Publishing Group UK 06.04.2023
Nature Publishing Group
Subjects:
101/28
631/326/193
631/45/221
631/535/1258/1259
82/16
82/80
82/83
Antifungal agents
Antifungal Agents - pharmacology
beta-Glucans - metabolism
Biosynthesis
Catalytic Domain
Cell Membrane - chemistry
Cell Membrane - metabolism
Cryoelectron Microscopy
Cytoplasm
Drug delivery
Drug resistance
Drug Resistance, Fungal - drug effects
Drug Resistance, Fungal - genetics
Drugs
Echinocandins
Echinocandins - pharmacology
Electron microscopy
Enzymes
Fungi
Fungicides
Glucan
Glucosyltransferases - antagonists & inhibitors
Glucosyltransferases - chemistry
Glucosyltransferases - genetics
Glucosyltransferases - metabolism
Glucosyltransferases - ultrastructure
Humanities and Social Sciences
Lipids
Membranes
Microbial Sensitivity Tests
Microscopy
multidisciplinary
Mutation
Polymers
Resistant mutant
Saccharomyces cerevisiae - drug effects
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae Proteins - antagonists & inhibitors
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Saccharomyces cerevisiae Proteins - ultrastructure
Science
Science (multidisciplinary)
Translocation
β-1,3-Glucan
ISSN:0028-0836, 1476-4687, 1476-4687
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Abstract The membrane-integrated synthase FKS is involved in the biosynthesis of β-1,3-glucan, the core component of the fungal cell wall 1 , 2 . FKS is the target of widely prescribed antifungal drugs, including echinocandin and ibrexafungerp 3 , 4 . Unfortunately, the mechanism of action of FKS remains enigmatic and this has hampered development of more effective medicines targeting the enzyme. Here we present the cryo-electron microscopy structures of Saccharomyces cerevisiae FKS1 and the echinocandin-resistant mutant FKS1(S643P). These structures reveal the active site of the enzyme at the membrane–cytoplasm interface and a glucan translocation path spanning the membrane bilayer. Multiple bound lipids and notable membrane distortions are observed in the FKS1 structures, suggesting active FKS1–membrane interactions. Echinocandin-resistant mutations are clustered at a region near TM5–6 and TM8 of FKS1. The structure of FKS1(S643P) reveals altered lipid arrangements in this region, suggesting a drug-resistant mechanism of the mutant enzyme. The structures, the catalytic mechanism and the molecular insights into drug-resistant mutations of FKS1 revealed in this study advance the mechanistic understanding of fungal β-1,3-glucan biosynthesis and establish a foundation for developing new antifungal drugs by targeting FKS. Using cryo-electron microscopy, the molecular architecture and catalytic mechanism of action of the fungal β-1,3-glucan synthase FKS1 are determined.
AbstractList The membrane-integrated synthase FKS is involved in the biosynthesis of β-1,3-glucan, the core component of the fungal cell wall1,2. FKS is the target of widely prescribed antifungal drugs, including echinocandin and ibrexafungerp3,4. Unfortunately, the mechanism of action of FKS remains enigmatic and this has hampered development of more effective medicines targeting the enzyme. Here we present the cryo-electron microscopy structures of Saccharomyces cerevisiae FKS1 and the echinocandin-resistant mutant FKS1(S643P). These structures reveal the active site of the enzyme at the membrane-cytoplasm interface and a glucan translocation path spanning the membrane bilayer. Multiple bound lipids and notable membrane distortions are observed in the FKS1 structures, suggesting active FKS1-membrane interactions. Echinocandin-resistant mutations are clustered at a region near TM5-6 and TM8 of FKS1. The structure of FKS1(S643P) reveals altered lipid arrangements in this region, suggesting a drug-resistant mechanism of the mutant enzyme. The structures, the catalytic mechanism and the molecular insights into drug-resistant mutations of FKS1 revealed in this study advance the mechanistic understanding of fungal β-1,3-glucan biosynthesis and establish a foundation for developing new antifungal drugs by targeting FKS.The membrane-integrated synthase FKS is involved in the biosynthesis of β-1,3-glucan, the core component of the fungal cell wall1,2. FKS is the target of widely prescribed antifungal drugs, including echinocandin and ibrexafungerp3,4. Unfortunately, the mechanism of action of FKS remains enigmatic and this has hampered development of more effective medicines targeting the enzyme. Here we present the cryo-electron microscopy structures of Saccharomyces cerevisiae FKS1 and the echinocandin-resistant mutant FKS1(S643P). These structures reveal the active site of the enzyme at the membrane-cytoplasm interface and a glucan translocation path spanning the membrane bilayer. Multiple bound lipids and notable membrane distortions are observed in the FKS1 structures, suggesting active FKS1-membrane interactions. Echinocandin-resistant mutations are clustered at a region near TM5-6 and TM8 of FKS1. The structure of FKS1(S643P) reveals altered lipid arrangements in this region, suggesting a drug-resistant mechanism of the mutant enzyme. The structures, the catalytic mechanism and the molecular insights into drug-resistant mutations of FKS1 revealed in this study advance the mechanistic understanding of fungal β-1,3-glucan biosynthesis and establish a foundation for developing new antifungal drugs by targeting FKS.
The membrane-integrated synthase FKS is involved in the biosynthesis of ß-1, 3-glucan, the core component of the fungal cell wall1,2. FKS is the target of widely prescribed antifungal drugs, including echinocandin and ibrexafungerp3,4. Unfortunately, the mechanism of action of FKS remains enigmatic and this has hampered development of more effective medicines targeting the enzyme. Here we present the cryo-electron microscopy structures of Saccharomyces cerevisiae FKS1 and the echinocandin-resistant mutant FKS1(S643P). These structures reveal the active site of the enzyme at the membrane-cytoplasm interface and a glucan translocation path spanning the membrane bilayer. Multiple bound lipids and notable membrane distortions are observed in the FKS1 structures, suggesting active FKS1-membrane interactions. Echinocandin-resistant mutations are clustered at a region near TM5-6 and TM8 of FKS1. The structure of FKS1(S643P) reveals altered lipid arrangements in this region, suggesting a drug-resistant mechanism of the mutant enzyme. The structures, the catalytic mechanism and the molecular insights into drug-resistant mutations of FKS1 revealed in this study advance the mechanistic understanding of fungal ß-1,3-glucan biosynthesis and establish a foundation for developing new antifungal drugs by targeting FKS.
The membrane-integrated synthase FKS is involved in the biosynthesis of β-1,3-glucan, the core component of the fungal cell wall1,2. FKS is the target of widely prescribed antifungal drugs, including echinocandin and ibrexafungerp3,4. Unfortunately, the mechanism of action of FKS remains enigmatic and this has hampered development of more effective medicines targeting the enzyme. Here we present the cryo-electron microscopy structures of Saccharomyces cerevisiae FKS1 and the echinocandin-resistant mutant FKS1(S643P). These structures reveal the active site of the enzyme at the membrane–cytoplasm interface and a glucan translocation path spanning the membrane bilayer. Multiple bound lipids and notable membrane distortions are observed in the FKS1 structures, suggesting active FKS1–membrane interactions. Echinocandin-resistant mutations are clustered at a region near TM5–6 and TM8 of FKS1. The structure of FKS1(S643P) reveals altered lipid arrangements in this region, suggesting a drug-resistant mechanism of the mutant enzyme. The structures, the catalytic mechanism and the molecular insights into drug-resistant mutations of FKS1 revealed in this study advance the mechanistic understanding of fungal β-1,3-glucan biosynthesis and establish a foundation for developing new antifungal drugs by targeting FKS. Using cryo-electron microscopy, the molecular architecture and catalytic mechanism of action of the fungal β-1,3-glucan synthase FKS1 are determined.
The membrane-integrated synthase FKS is involved in the biosynthesis of β-1,3-glucan, the core component of the fungal cell wall 1 , 2 . FKS is the target of widely prescribed antifungal drugs, including echinocandin and ibrexafungerp 3 , 4 . Unfortunately, the mechanism of action of FKS remains enigmatic and this has hampered development of more effective medicines targeting the enzyme. Here we present the cryo-electron microscopy structures of Saccharomyces cerevisiae FKS1 and the echinocandin-resistant mutant FKS1(S643P). These structures reveal the active site of the enzyme at the membrane–cytoplasm interface and a glucan translocation path spanning the membrane bilayer. Multiple bound lipids and notable membrane distortions are observed in the FKS1 structures, suggesting active FKS1–membrane interactions. Echinocandin-resistant mutations are clustered at a region near TM5–6 and TM8 of FKS1. The structure of FKS1(S643P) reveals altered lipid arrangements in this region, suggesting a drug-resistant mechanism of the mutant enzyme. The structures, the catalytic mechanism and the molecular insights into drug-resistant mutations of FKS1 revealed in this study advance the mechanistic understanding of fungal β-1,3-glucan biosynthesis and establish a foundation for developing new antifungal drugs by targeting FKS. Using cryo-electron microscopy, the molecular architecture and catalytic mechanism of action of the fungal β-1,3-glucan synthase FKS1 are determined.
The membrane-integrated synthase FKS is involved in the biosynthesis of β-1,3-glucan, the core component of the fungal cell wall . FKS is the target of widely prescribed antifungal drugs, including echinocandin and ibrexafungerp . Unfortunately, the mechanism of action of FKS remains enigmatic and this has hampered development of more effective medicines targeting the enzyme. Here we present the cryo-electron microscopy structures of Saccharomyces cerevisiae FKS1 and the echinocandin-resistant mutant FKS1(S643P). These structures reveal the active site of the enzyme at the membrane-cytoplasm interface and a glucan translocation path spanning the membrane bilayer. Multiple bound lipids and notable membrane distortions are observed in the FKS1 structures, suggesting active FKS1-membrane interactions. Echinocandin-resistant mutations are clustered at a region near TM5-6 and TM8 of FKS1. The structure of FKS1(S643P) reveals altered lipid arrangements in this region, suggesting a drug-resistant mechanism of the mutant enzyme. The structures, the catalytic mechanism and the molecular insights into drug-resistant mutations of FKS1 revealed in this study advance the mechanistic understanding of fungal β-1,3-glucan biosynthesis and establish a foundation for developing new antifungal drugs by targeting FKS.
Author Yang, Ping
Sun, Huanhuan
Yu, Hongjun
Zhang, Mingjie
Liu, Xiaotian
Hu, Xinlin
Liu, Jia
Chai, Changdong
Wu, Yanan
Zhang, Min
Author_xml – sequence: 1
  givenname: Xinlin
  surname: Hu
  fullname: Hu, Xinlin
  organization: Department of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Department of Pathogen Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology
– sequence: 2
  givenname: Ping
  surname: Yang
  fullname: Yang, Ping
  organization: Department of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology
– sequence: 3
  givenname: Changdong
  surname: Chai
  fullname: Chai, Changdong
  organization: Department of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology
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  givenname: Jia
  surname: Liu
  fullname: Liu, Jia
  organization: Department of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Department of Pathogen Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology
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  organization: Department of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology
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  surname: Wu
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  organization: Department of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology
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  surname: Zhang
  fullname: Zhang, Mingjie
  organization: School of Life Sciences, Southern University of Science and Technology, Greater Bay Biomedical Innocenter, Shenzhen Bay Laboratory
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  givenname: Min
  orcidid: 0000-0002-8844-8402
  surname: Zhang
  fullname: Zhang, Min
  email: minzhang@hust.edu.cn
  organization: Department of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Department of Pathogen Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology
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  fullname: Yu, Hongjun
  email: hongjun_yu@hust.edu.cn
  organization: Department of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Cell Architecture Research Center, Huazhong University of Science and Technology
BackLink https://www.ncbi.nlm.nih.gov/pubmed/36949198$$D View this record in MEDLINE/PubMed
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Cites_doi 10.2165/11585270-000000000-00000
10.1016/j.tcb.2021.01.002
10.1073/pnas.1611173113
10.1128/mBio.03333-20
10.1021/acs.biochem.9b00896
10.1002/jcc.20084
10.1128/AAC.02299-17
10.1038/nmeth.2727
10.1128/AAC.49.8.3264-3273.2005
10.1146/annurev.biochem.76.061005.092322
10.1128/JB.181.2.444-453.1999
10.1093/cid/cit136
10.7554/eLife.42166
10.1107/S2059798318009324
10.1007/s40265-021-01611-0
10.1002/yea.1658
10.1038/nrd.2017.46
10.1128/mBio.00779-19
10.1007/s40265-014-0286-5
10.1126/science.aap7999
10.1126/scitranslmed.3004404
10.1093/glycob/9.1.31
10.1016/j.tcsw.2018.09.001
10.1128/AEM.02728-08
10.1107/S0907444909042073
10.1111/nyas.12831
10.1016/j.jmb.2020.06.016
10.1111/j.1365-2958.2012.08194.x
10.1128/EC.00082-12
10.1016/0008-6215(84)85242-8
10.1107/S0907444909052925
10.1002/pro.3943
10.1126/science.abb2978
10.1002/yea.742
10.1128/AAC.41.11.2471
10.1128/JB.183.7.2273-2279.2001
10.1038/nsmb.2803
10.1038/s41586-021-03819-2
10.1128/AAC.00813-12
10.1107/S0907444910007493
10.1093/nar/gkw357
10.1042/BJ20082117
10.1128/microbiolspec.FUNK-0035-2016
10.1099/13500872-140-9-2239
10.1038/nmeth.4193
10.1111/j.1399-3054.1990.tb02096.x
10.1111/mmi.12877
10.1093/nar/gkab1061
10.1016/j.jsb.2015.08.008
10.3109/13693786.2012.675525
10.1021/bm050799c
10.1093/genetics/162.2.663
10.1093/cid/ciaa1342
10.1007/s00253-005-1959-5
10.1128/AAC.01610-05
10.1016/j.sbi.2015.07.008
10.1126/science.272.5259.279
10.1038/nprot.2006.468
10.1016/j.cell.2020.02.056
10.1128/MCB.15.10.5671
10.1038/nature11744
10.1128/AAC.00833-17
10.1128/AAC.01811-10
10.1016/j.jmb.2003.07.013
10.1111/j.1432-1033.1995.tb20770.x
10.1073/pnas.91.26.12907
10.1038/s41586-022-04534-2
10.1016/S1473-3099(17)30316-X
10.1002/yea.1397
10.1006/abio.1997.2162
10.1074/jbc.271.24.14604
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References PD Adams (5856_CR55) 2010; 66
M Hoenigl (5856_CR6) 2021; 73
DS Perlin (5856_CR9) 2020; 425
YH Zhang (5856_CR64) 2006; 7
JR Perfect (5856_CR3) 2017; 16
JR Thompson (5856_CR16) 1999; 181
M Sekiya-Kawasaki (5856_CR69) 2002; 162
DS Perlin (5856_CR20) 2015; 1354
A Shevchenko (5856_CR73) 2006; 1
SB Inoue (5856_CR10) 1995; 231
H Carolus (5856_CR40) 2021; 12
P Mazur (5856_CR13) 1996; 271
FP Maloney (5856_CR34) 2022; 604
ME Johnson (5856_CR24) 2012; 11
I Ciucanu (5856_CR66) 1984; 131
Y Bi (5856_CR38) 2015; 34
P Mazur (5856_CR15) 1995; 15
S Park (5856_CR23) 2005; 49
K Dichtl (5856_CR18) 2015; 95
SK Katiyar (5856_CR14) 2012; 56
DS Perlin (5856_CR28) 2014; 74
M McIntosh (5856_CR65) 2005; 68
SJ Stasinopoulos (5856_CR37) 1999; 9
ME Johnson (5856_CR22) 2011; 55
A Chhetri (5856_CR25) 2020; 59
SC Chen (5856_CR19) 2011; 71
P Emsley (5856_CR56) 2010; 66
C Jimenez-Ortigosa (5856_CR41) 2017; 61
A Beauvais (5856_CR27) 2001; 183
GD Brown (5856_CR5) 2012; 4
H Qadota (5856_CR12) 1996; 272
P Purushotham (5856_CR33) 2020; 369
S Suwunnakorn (5856_CR26) 2018; 62
L Holm (5856_CR59) 2016; 44
NAR Gow (5856_CR2) 2017
EF Pettersen (5856_CR63) 2021; 30
LL Lairson (5856_CR31) 2008; 77
JT Mullins (5856_CR29) 1990; 78
JL Morgan (5856_CR32) 2014; 21
L Bessueille (5856_CR44) 2009; 420
J Wagener (5856_CR1) 2020; 425
A Toulmay (5856_CR49) 2006; 23
A Rohou (5856_CR51) 2015; 192
J Jumper (5856_CR60) 2021; 596
DS Perlin (5856_CR7) 2017; 17
K Lewis (5856_CR43) 2020; 181
DJ Frost (5856_CR30) 1994; 140
KR Healey (5856_CR46) 2012; 86
CM Douglas (5856_CR11) 1994; 91
A Kucukelbir (5856_CR54) 2014; 11
JL Morgan (5856_CR36) 2013; 493
CM Douglas (5856_CR17) 1997; 41
KK Lee (5856_CR71) 2018; 3
MC Fisher (5856_CR8) 2018; 360
A Briolay (5856_CR45) 2009; 75
EF Pettersen (5856_CR62) 2004; 25
JN Kahn (5856_CR68) 2006; 50
A Muller (5856_CR42) 2016; 113
M Varadi (5856_CR61) 2022; 50
S Satish (5856_CR47) 2019; 10
E Shedletzky (5856_CR67) 1997; 249
J Zivanov (5856_CR52) 2018; 7
R Gandini (5856_CR35) 2020; 432
D Watanabe (5856_CR70) 2001; 18
SQ Zheng (5856_CR50) 2017; 14
VB Chen (5856_CR57) 2010; 66
BD Alexander (5856_CR21) 2013; 56
PV Afonine (5856_CR58) 2018; 74
M Funakoshi (5856_CR48) 2009; 26
PB Rosenthal (5856_CR53) 2003; 333
M Hoenigl (5856_CR4) 2021; 81
J Anjos (5856_CR72) 2012; 50
XD Wu (5856_CR39) 2021; 31
References_xml – volume: 71
  start-page: 11
  year: 2011
  ident: 5856_CR19
  publication-title: Drugs
  doi: 10.2165/11585270-000000000-00000
– volume: 31
  start-page: 473
  year: 2021
  ident: 5856_CR39
  publication-title: Trends Cell Biol.
  doi: 10.1016/j.tcb.2021.01.002
– volume: 113
  start-page: E7077
  year: 2016
  ident: 5856_CR42
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.1611173113
– volume: 12
  start-page: e03333-20
  year: 2021
  ident: 5856_CR40
  publication-title: mBio
  doi: 10.1128/mBio.03333-20
– volume: 59
  start-page: 682
  year: 2020
  ident: 5856_CR25
  publication-title: Biochemistry
  doi: 10.1021/acs.biochem.9b00896
– volume: 25
  start-page: 1605
  year: 2004
  ident: 5856_CR62
  publication-title: J. Comput. Chem.
  doi: 10.1002/jcc.20084
– volume: 62
  start-page: e02299-17
  year: 2018
  ident: 5856_CR26
  publication-title: Antimicrob. Agents Chemother.
  doi: 10.1128/AAC.02299-17
– volume: 11
  start-page: 63
  year: 2014
  ident: 5856_CR54
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.2727
– volume: 49
  start-page: 3264
  year: 2005
  ident: 5856_CR23
  publication-title: Antimicrob. Agents Chemother.
  doi: 10.1128/AAC.49.8.3264-3273.2005
– volume: 77
  start-page: 521
  year: 2008
  ident: 5856_CR31
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.76.061005.092322
– volume: 181
  start-page: 444
  year: 1999
  ident: 5856_CR16
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.181.2.444-453.1999
– volume: 56
  start-page: 1724
  year: 2013
  ident: 5856_CR21
  publication-title: Clin. Infect. Dis.
  doi: 10.1093/cid/cit136
– volume: 7
  start-page: e42166
  year: 2018
  ident: 5856_CR52
  publication-title: eLife
  doi: 10.7554/eLife.42166
– volume: 74
  start-page: 814
  year: 2018
  ident: 5856_CR58
  publication-title: Acta Crystallogr. D Struct. Biol.
  doi: 10.1107/S2059798318009324
– volume: 81
  start-page: 1703
  year: 2021
  ident: 5856_CR4
  publication-title: Drugs
  doi: 10.1007/s40265-021-01611-0
– volume: 26
  start-page: 185
  year: 2009
  ident: 5856_CR48
  publication-title: Yeast
  doi: 10.1002/yea.1658
– volume: 16
  start-page: 603
  year: 2017
  ident: 5856_CR3
  publication-title: Nat. Rev. Drug Discov.
  doi: 10.1038/nrd.2017.46
– volume: 10
  start-page: e00779-19
  year: 2019
  ident: 5856_CR47
  publication-title: mBio
  doi: 10.1128/mBio.00779-19
– volume: 74
  start-page: 1573
  year: 2014
  ident: 5856_CR28
  publication-title: Drugs
  doi: 10.1007/s40265-014-0286-5
– volume: 360
  start-page: 739
  year: 2018
  ident: 5856_CR8
  publication-title: Science
  doi: 10.1126/science.aap7999
– volume: 4
  start-page: 165rv113
  year: 2012
  ident: 5856_CR5
  publication-title: Sci. Transl. Med.
  doi: 10.1126/scitranslmed.3004404
– volume: 9
  start-page: 31
  year: 1999
  ident: 5856_CR37
  publication-title: Glycobiology
  doi: 10.1093/glycob/9.1.31
– volume: 3
  start-page: 12
  year: 2018
  ident: 5856_CR71
  publication-title: Cell Surf.
  doi: 10.1016/j.tcsw.2018.09.001
– volume: 75
  start-page: 1938
  year: 2009
  ident: 5856_CR45
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.02728-08
– volume: 66
  start-page: 12
  year: 2010
  ident: 5856_CR57
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  doi: 10.1107/S0907444909042073
– volume: 1354
  start-page: 1
  year: 2015
  ident: 5856_CR20
  publication-title: Ann. N.Y. Acad. Sci.
  doi: 10.1111/nyas.12831
– volume: 432
  start-page: 4658
  year: 2020
  ident: 5856_CR35
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2020.06.016
– volume: 86
  start-page: 303
  year: 2012
  ident: 5856_CR46
  publication-title: Mol. Microbiol.
  doi: 10.1111/j.1365-2958.2012.08194.x
– volume: 11
  start-page: 952
  year: 2012
  ident: 5856_CR24
  publication-title: Eukaryot. Cell
  doi: 10.1128/EC.00082-12
– volume: 131
  start-page: 209
  year: 1984
  ident: 5856_CR66
  publication-title: Carbohydr. Res.
  doi: 10.1016/0008-6215(84)85242-8
– volume: 66
  start-page: 213
  year: 2010
  ident: 5856_CR55
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  doi: 10.1107/S0907444909052925
– volume: 30
  start-page: 70
  year: 2021
  ident: 5856_CR63
  publication-title: Protein Sci.
  doi: 10.1002/pro.3943
– volume: 369
  start-page: 1089
  year: 2020
  ident: 5856_CR33
  publication-title: Science
  doi: 10.1126/science.abb2978
– volume: 18
  start-page: 943
  year: 2001
  ident: 5856_CR70
  publication-title: Yeast
  doi: 10.1002/yea.742
– volume: 41
  start-page: 2471
  year: 1997
  ident: 5856_CR17
  publication-title: Antimicrob. Agents Chemother.
  doi: 10.1128/AAC.41.11.2471
– volume: 183
  start-page: 2273
  year: 2001
  ident: 5856_CR27
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.183.7.2273-2279.2001
– volume: 21
  start-page: 489
  year: 2014
  ident: 5856_CR32
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.2803
– volume: 596
  start-page: 583
  year: 2021
  ident: 5856_CR60
  publication-title: Nature
  doi: 10.1038/s41586-021-03819-2
– volume: 56
  start-page: 6304
  year: 2012
  ident: 5856_CR14
  publication-title: Antimicrob. Agents Chemother.
  doi: 10.1128/AAC.00813-12
– volume: 66
  start-page: 486
  year: 2010
  ident: 5856_CR56
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  doi: 10.1107/S0907444910007493
– volume: 44
  start-page: W351
  year: 2016
  ident: 5856_CR59
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkw357
– volume: 420
  start-page: 93
  year: 2009
  ident: 5856_CR44
  publication-title: Biochem. J.
  doi: 10.1042/BJ20082117
– year: 2017
  ident: 5856_CR2
  publication-title: Microbiol. Spect.
  doi: 10.1128/microbiolspec.FUNK-0035-2016
– volume: 140
  start-page: 2239
  year: 1994
  ident: 5856_CR30
  publication-title: Microbiology
  doi: 10.1099/13500872-140-9-2239
– volume: 425
  start-page: 255
  year: 2020
  ident: 5856_CR9
  publication-title: Curr. Top. Microbiol. Immunol.
– volume: 14
  start-page: 331
  year: 2017
  ident: 5856_CR50
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.4193
– volume: 78
  start-page: 309
  year: 1990
  ident: 5856_CR29
  publication-title: Physiol. Plant.
  doi: 10.1111/j.1399-3054.1990.tb02096.x
– volume: 95
  start-page: 458
  year: 2015
  ident: 5856_CR18
  publication-title: Mol. Microbiol.
  doi: 10.1111/mmi.12877
– volume: 50
  start-page: D439
  year: 2022
  ident: 5856_CR61
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkab1061
– volume: 192
  start-page: 216
  year: 2015
  ident: 5856_CR51
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2015.08.008
– volume: 50
  start-page: 716
  year: 2012
  ident: 5856_CR72
  publication-title: Med. Mycol.
  doi: 10.3109/13693786.2012.675525
– volume: 7
  start-page: 644
  year: 2006
  ident: 5856_CR64
  publication-title: Biomacromolecules
  doi: 10.1021/bm050799c
– volume: 162
  start-page: 663
  year: 2002
  ident: 5856_CR69
  publication-title: Genetics
  doi: 10.1093/genetics/162.2.663
– volume: 73
  start-page: e1645
  year: 2021
  ident: 5856_CR6
  publication-title: Clin. Infect. Dis.
  doi: 10.1093/cid/ciaa1342
– volume: 68
  start-page: 163
  year: 2005
  ident: 5856_CR65
  publication-title: Appl. Microbiol. Biot.
  doi: 10.1007/s00253-005-1959-5
– volume: 425
  start-page: 53
  year: 2020
  ident: 5856_CR1
  publication-title: Curr. Top. Microbiol. Immunol.
– volume: 50
  start-page: 2214
  year: 2006
  ident: 5856_CR68
  publication-title: Antimicrob. Agents Chemother.
  doi: 10.1128/AAC.01610-05
– volume: 34
  start-page: 78
  year: 2015
  ident: 5856_CR38
  publication-title: Curr. Opin. Struct. Biol.
  doi: 10.1016/j.sbi.2015.07.008
– volume: 272
  start-page: 279
  year: 1996
  ident: 5856_CR12
  publication-title: Science
  doi: 10.1126/science.272.5259.279
– volume: 1
  start-page: 2856
  year: 2006
  ident: 5856_CR73
  publication-title: Nat. Protoc.
  doi: 10.1038/nprot.2006.468
– volume: 181
  start-page: 29
  year: 2020
  ident: 5856_CR43
  publication-title: Cell
  doi: 10.1016/j.cell.2020.02.056
– volume: 15
  start-page: 5671
  year: 1995
  ident: 5856_CR15
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.15.10.5671
– volume: 493
  start-page: 181
  year: 2013
  ident: 5856_CR36
  publication-title: Nature
  doi: 10.1038/nature11744
– volume: 61
  start-page: e00833-17
  year: 2017
  ident: 5856_CR41
  publication-title: Antimicrob. Agents Chemother.
  doi: 10.1128/AAC.00833-17
– volume: 55
  start-page: 3774
  year: 2011
  ident: 5856_CR22
  publication-title: Antimicrob. Agents Chemother.
  doi: 10.1128/AAC.01811-10
– volume: 333
  start-page: 721
  year: 2003
  ident: 5856_CR53
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2003.07.013
– volume: 231
  start-page: 845
  year: 1995
  ident: 5856_CR10
  publication-title: Eur. J. Biochem.
  doi: 10.1111/j.1432-1033.1995.tb20770.x
– volume: 91
  start-page: 12907
  year: 1994
  ident: 5856_CR11
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.91.26.12907
– volume: 604
  start-page: 195
  year: 2022
  ident: 5856_CR34
  publication-title: Nature
  doi: 10.1038/s41586-022-04534-2
– volume: 17
  start-page: e383
  year: 2017
  ident: 5856_CR7
  publication-title: Lancet Infect. Dis.
  doi: 10.1016/S1473-3099(17)30316-X
– volume: 23
  start-page: 825
  year: 2006
  ident: 5856_CR49
  publication-title: Yeast
  doi: 10.1002/yea.1397
– volume: 249
  start-page: 88
  year: 1997
  ident: 5856_CR67
  publication-title: Anal. Biochem.
  doi: 10.1006/abio.1997.2162
– volume: 271
  start-page: 14604
  year: 1996
  ident: 5856_CR13
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.271.24.14604
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Snippet The membrane-integrated synthase FKS is involved in the biosynthesis of β-1,3-glucan, the core component of the fungal cell wall 1 , 2 . FKS is the target of...
The membrane-integrated synthase FKS is involved in the biosynthesis of β-1,3-glucan, the core component of the fungal cell wall . FKS is the target of widely...
The membrane-integrated synthase FKS is involved in the biosynthesis of ß-1, 3-glucan, the core component of the fungal cell wall1,2. FKS is the target of...
The membrane-integrated synthase FKS is involved in the biosynthesis of β-1,3-glucan, the core component of the fungal cell wall1,2. FKS is the target of...
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StartPage 190
SubjectTerms 101/28
631/326/193
631/45/221
631/535/1258/1259
82/16
82/80
82/83
Antifungal agents
Antifungal Agents - pharmacology
beta-Glucans - metabolism
Biosynthesis
Catalytic Domain
Cell Membrane - chemistry
Cell Membrane - metabolism
Cryoelectron Microscopy
Cytoplasm
Drug delivery
Drug resistance
Drug Resistance, Fungal - drug effects
Drug Resistance, Fungal - genetics
Drugs
Echinocandins
Echinocandins - pharmacology
Electron microscopy
Enzymes
Fungi
Fungicides
Glucan
Glucosyltransferases - antagonists & inhibitors
Glucosyltransferases - chemistry
Glucosyltransferases - genetics
Glucosyltransferases - metabolism
Glucosyltransferases - ultrastructure
Humanities and Social Sciences
Lipids
Membranes
Microbial Sensitivity Tests
Microscopy
multidisciplinary
Mutation
Polymers
Resistant mutant
Saccharomyces cerevisiae - drug effects
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae Proteins - antagonists & inhibitors
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Saccharomyces cerevisiae Proteins - ultrastructure
Science
Science (multidisciplinary)
Translocation
β-1,3-Glucan
Title Structural and mechanistic insights into fungal β-1,3-glucan synthase FKS1
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