Crystal structures of SARS-CoV-2 ADP-ribose phosphatase: from the apo form to ligand complexes

Among 15 nonstructural proteins (Nsps), the newly emerging Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) encodes a large, multidomain Nsp3. One of its units is the ADP-ribose phosphatase domain (ADRP; also known as the macrodomain, MacroD), which is believed to interfere with the host...

Celý popis

Uložené v:

Podrobná bibliografia
Vydané v:	IUCrJ Ročník 7; číslo 5; s. 814 - 824
Hlavní autori:	Michalska, Karolina, Kim, Youngchang, Jedrzejczak, Robert, Maltseva, Natalia I., Stols, Lucy, Endres, Michael, Joachimiak, Andrzej
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	England International Union of Crystallography 01.09.2020
Predmet:	ADP-ribose phosphatase domain ADP-ribosylation ADRP BASIC BIOLOGICAL SCIENCES Coordination compounds Coronaviruses COVID-19 Crystal structure Enzymes Health aspects Homology Ligands Mac1 macrodomain Monosaccharides Nsp3 Phosphatase Phosphatases Proteins Research Papers Ribose RNA SARS-CoV-2 Severe acute respiratory syndrome Severe acute respiratory syndrome coronavirus 2 Viral diseases Water chemistry COVID-19 SARS-CoV-2 Mac1 crystal structure macrodomain ADP-ribose phosphatase domain Nsp3 ADP-ribosylation ADRP
ISSN:	2052-2525, 2052-2525
On-line prístup:	Získať plný text
Tagy:	Pridať tag Žiadne tagy, Buďte prvý, kto otaguje tento záznam!

Abstract	Among 15 nonstructural proteins (Nsps), the newly emerging Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) encodes a large, multidomain Nsp3. One of its units is the ADP-ribose phosphatase domain (ADRP; also known as the macrodomain, MacroD), which is believed to interfere with the host immune response. Such a function appears to be linked to the ability of the protein to remove ADP-ribose from ADP-ribosylated proteins and RNA, yet the precise role and molecular targets of the enzyme remain unknown. Here, five high-resolution (1.07–2.01 Å) crystal structures corresponding to the apo form of the protein and its complexes with 2-( N -morpholino)ethanesulfonic acid (MES), AMP and ADP-ribose have been determined. The protein is shown to undergo conformational changes to adapt to the ligand in the manner previously observed in close homologues from other viruses. A conserved water molecule is also identified that may participate in hydrolysis. This work builds foundations for future structure-based research on ADRP, including the search for potential antiviral therapeutics.
AbstractList	Among 15 nonstructural proteins (Nsps), the newly emerging Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) encodes a large, multidomain Nsp3. One of its units is the ADP-ribose phosphatase domain (ADRP; also known as the macrodomain, MacroD), which is believed to interfere with the host immune response. Such a function appears to be linked to the ability of the protein to remove ADP-ribose from ADP-ribosylated proteins and RNA, yet the precise role and molecular targets of the enzyme remain unknown. Here, five high-resolution (1.07-2.01 Å) crystal structures corresponding to the apo form of the protein and its complexes with 2-(N-morpholino)ethanesulfonic acid (MES), AMP and ADP-ribose have been determined. The protein is shown to undergo conformational changes to adapt to the ligand in the manner previously observed in close homologues from other viruses. A conserved water molecule is also identified that may participate in hydrolysis. This work builds foundations for future structure-based research on ADRP, including the search for potential antiviral therapeutics.Among 15 nonstructural proteins (Nsps), the newly emerging Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) encodes a large, multidomain Nsp3. One of its units is the ADP-ribose phosphatase domain (ADRP; also known as the macrodomain, MacroD), which is believed to interfere with the host immune response. Such a function appears to be linked to the ability of the protein to remove ADP-ribose from ADP-ribosylated proteins and RNA, yet the precise role and molecular targets of the enzyme remain unknown. Here, five high-resolution (1.07-2.01 Å) crystal structures corresponding to the apo form of the protein and its complexes with 2-(N-morpholino)ethanesulfonic acid (MES), AMP and ADP-ribose have been determined. The protein is shown to undergo conformational changes to adapt to the ligand in the manner previously observed in close homologues from other viruses. A conserved water molecule is also identified that may participate in hydrolysis. This work builds foundations for future structure-based research on ADRP, including the search for potential antiviral therapeutics. Among 15 nonstructural proteins (Nsps), the newly emerging Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) encodes a large, multidomain Nsp3. One of its units is the ADP-ribose phosphatase domain (ADRP; also known as the macrodomain, MacroD), which is believed to interfere with the host immune response. Such a function appears to be linked to the ability of the protein to remove ADP-ribose from ADP-ribosylated proteins and RNA, yet the precise role and molecular targets of the enzyme remain unknown. Here, five high-resolution (1.07–2.01 Å) crystal structures corresponding to the apo form of the protein and its complexes with 2-( N -morpholino)ethanesulfonic acid (MES), AMP and ADP-ribose have been determined. The protein is shown to undergo conformational changes to adapt to the ligand in the manner previously observed in close homologues from other viruses. A conserved water molecule is also identified that may participate in hydrolysis. This work builds foundations for future structure-based research on ADRP, including the search for potential antiviral therapeutics. Among 15 nonstructural proteins (Nsps), the newly emerging Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) encodes a large, multidomain Nsp3. One of its units is the ADP-ribose phosphatase domain (ADRP; also known as the macrodomain, MacroD), which is believed to interfere with the host immune response. Such a function appears to be linked to the ability of the protein to remove ADP-ribose from ADP-ribosylated proteins and RNA, yet the precise role and molecular targets of the enzyme remain unknown. Here, five high-resolution (1.07-2.01 Å) crystal structures corresponding to the apo form of the protein and its complexes with 2-( -morpholino)ethanesulfonic acid (MES), AMP and ADP-ribose have been determined. The protein is shown to undergo conformational changes to adapt to the ligand in the manner previously observed in close homologues from other viruses. A conserved water molecule is also identified that may participate in hydrolysis. This work builds foundations for future structure-based research on ADRP, including the search for potential antiviral therapeutics. Among 15 nonstructural proteins (Nsps), the newly emerging Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) encodes a large, multidomain Nsp3. One of its units is the ADP-ribose phosphatase domain (ADRP; also known as the macrodomain, MacroD), which is believed to interfere with the host immune response. Such a function appears to be linked to the ability of the protein to remove ADP-ribose from ADP-ribosylated proteins and RNA, yet the precise role and molecular targets of the enzyme remain unknown. Here, five high-resolution (1.07–2.01 Å) crystal structures corresponding to the apo form of the protein and its complexes with 2-(N-morpholino)ethanesulfonic acid (MES), AMP and ADP-ribose have been determined. The protein is shown to undergo conformational changes to adapt to the ligand in the manner previously observed in close homologues from other viruses. A conserved water molecule is also identified that may participate in hydrolysis. This work builds foundations for future structure-based research on ADRP, including the search for potential antiviral therapeutics. High-resolution crystal structures of the ADP-ribose phosphatase domain (ADRP; also known as the macrodomain) from SARS-CoV-2 with multiple ligands illustrate how the protein undergoes conformational changes to adapt to the ligand in the manner observed for homologues from other viruses. Among 15 nonstructural proteins (Nsps), the newly emerging Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) encodes a large, multidomain Nsp3. One of its units is the ADP-ribose phosphatase domain (ADRP; also known as the macrodomain, MacroD), which is believed to interfere with the host immune response. Such a function appears to be linked to the ability of the protein to remove ADP-ribose from ADP-ribosylated proteins and RNA, yet the precise role and molecular targets of the enzyme remain unknown. Here, five high-resolution (1.07–2.01 Å) crystal structures corresponding to the apo form of the protein and its complexes with 2-(N-morpholino)ethanesulfonic acid (MES), AMP and ADP-ribose have been determined. The protein is shown to undergo conformational changes to adapt to the ligand in the manner previously observed in close homologues from other viruses. A conserved water molecule is also identified that may participate in hydrolysis. This work builds foundations for future structure-based research on ADRP, including the search for potential antiviral therapeutics.
Audience	Academic
Author	Maltseva, Natalia I. Endres, Michael Stols, Lucy Kim, Youngchang Jedrzejczak, Robert Michalska, Karolina Joachimiak, Andrzej
Author_xml	– sequence: 1 givenname: Karolina surname: Michalska fullname: Michalska, Karolina – sequence: 2 givenname: Youngchang surname: Kim fullname: Kim, Youngchang – sequence: 3 givenname: Robert surname: Jedrzejczak fullname: Jedrzejczak, Robert – sequence: 4 givenname: Natalia I. surname: Maltseva fullname: Maltseva, Natalia I. – sequence: 5 givenname: Lucy surname: Stols fullname: Stols, Lucy – sequence: 6 givenname: Michael surname: Endres fullname: Endres, Michael – sequence: 7 givenname: Andrzej orcidid: 0000-0003-2535-6209 surname: Joachimiak fullname: Joachimiak, Andrzej
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/32939273$$D View this record in MEDLINE/PubMed https://www.osti.gov/servlets/purl/1774292$$D View this record in Osti.gov
BookMark	eNp1kktv1DAQgCNUREvpD-CCIrhwSfEzTjhUWi2vSpVALHDEcuzxrqskDraD6L_Hy7bQLSAfYo-_-eIZzcPiYPQjFMVjjE4xRuLFiiBOCM8LIdTWnN4rjrahahs7uLU_LE5ivMwQxoQLhh8Uh5S0tCWCHhVfl-EqJtWXMYVZpzlALL0tV4uPq2rpv1SkXLz6UAXX-QjltPFx2qikIrwsbfBDmTZQqsmX1od88GXv1mo0pfbD1MMPiI-K-1b1EU6uv8fF5zevPy3fVRfv354vFxeV5ojQStNGaaRw1zDGUIsFNQAUGUPBGM6sNo1lAJYxJUhnhWiwQcABtZ2yDSh6XJzvvMarSzkFN6hwJb1y8lfAh7VUITndg9QdoryhtaUkm2vd4bZFNeWECuAKuuw627mmuRvAaBhTUP2edP9mdBu59t-lYLXAgmXB053Ax-Rk1C6B3mg_jqCTxEIw0pIMPb_-S_DfZohJDi5q6Hs1gp-jJIzRpuGoqTP67A566ecw5n5KUiPGcjFI_KHWKlfpRuvz4_RWKhc1rTmumaCZOv0HlZeBweU3gnU5vpfw5HY3frfhZoQyIHaADj7GAFbmglVyftsc10uM5HZe5V_zmjPxncwb-f9zfgKmOugc
CitedBy_id	crossref_primary_10_1128_JVI_01969_20 crossref_primary_10_1002_jobm_202000537 crossref_primary_10_1128_mbio_03865_24 crossref_primary_10_1016_j_crmeth_2021_100121 crossref_primary_10_1080_00268976_2024_2353331 crossref_primary_10_1128_jvi_01313_24 crossref_primary_10_1128_spectrum_02871_24 crossref_primary_10_1080_07391102_2021_1873191 crossref_primary_10_1080_00268976_2024_2390592 crossref_primary_10_1098_rsob_200237 crossref_primary_10_1038_s41598_024_81711_5 crossref_primary_10_1016_j_jmb_2020_11_024 crossref_primary_10_3390_antibiotics10050542 crossref_primary_10_1016_j_jbc_2021_101041 crossref_primary_10_1016_j_drudis_2021_05_007 crossref_primary_10_1007_s10930_020_09942_9 crossref_primary_10_1007_s12104_025_10227_4 crossref_primary_10_1111_jfbc_14219 crossref_primary_10_1038_s41598_022_08320_y crossref_primary_10_1107_S2052252521003948 crossref_primary_10_1186_s42269_021_00517_x crossref_primary_10_1080_07391102_2023_2226745 crossref_primary_10_1016_j_pbiomolbio_2021_02_002 crossref_primary_10_1093_bib_bbab484 crossref_primary_10_1177_03946320221142793 crossref_primary_10_1002_slct_202304761 crossref_primary_10_1016_j_ijbiomac_2024_134850 crossref_primary_10_1080_07391102_2023_2297005 crossref_primary_10_1016_j_omtn_2022_06_017 crossref_primary_10_1080_00268976_2023_2295427 crossref_primary_10_1080_0889311X_2022_2098281 crossref_primary_10_1002_jmv_27225 crossref_primary_10_3390_antibiotics10040420 crossref_primary_10_1111_febs_70039 crossref_primary_10_1016_j_poly_2024_117014 crossref_primary_10_3390_v15122291 crossref_primary_10_1007_s11356_022_22025_9 crossref_primary_10_1038_s41392_021_00718_w crossref_primary_10_1016_j_bbrc_2020_11_041 crossref_primary_10_1002_gepi_22515 crossref_primary_10_1038_s41392_022_00884_5 crossref_primary_10_1107_S205225252401217X crossref_primary_10_1128_jvi_01777_23 crossref_primary_10_3389_fmicb_2023_1291761 crossref_primary_10_1016_j_virol_2023_109845 crossref_primary_10_1016_j_virol_2023_02_011 crossref_primary_10_1016_j_drudis_2023_103832 crossref_primary_10_1073_pnas_2004500118 crossref_primary_10_1016_j_csbj_2021_08_036 crossref_primary_10_3390_cryst13091374 crossref_primary_10_1111_ijcp_13877 crossref_primary_10_3390_molecules27238287 crossref_primary_10_1016_j_compbiomed_2021_105084 crossref_primary_10_1016_j_scr_2021_102219 crossref_primary_10_3390_pathogens12070964 crossref_primary_10_1128_JVI_00766_21 crossref_primary_10_1093_pnasnexus_pgaf094 crossref_primary_10_1016_j_molstruc_2021_131892 crossref_primary_10_1016_j_coviro_2021_11_011 crossref_primary_10_1038_s41579_022_00839_1 crossref_primary_10_1042_BST20200396 crossref_primary_10_1007_s10930_021_09967_8 crossref_primary_10_1016_j_compbiomed_2020_104185 crossref_primary_10_1080_00268976_2024_2404244 crossref_primary_10_1073_pnas_2212931120 crossref_primary_10_1007_s00018_022_04290_6 crossref_primary_10_1016_j_jbc_2021_100747 crossref_primary_10_1080_07391102_2022_2112976 crossref_primary_10_1080_00268976_2024_2436095
Cites_doi	10.1128/JVI.00189-09 10.1107/S0907444910045749 10.1146/annurev-biochem-060815-014935 10.1074/jbc.M115.700542 10.1002/0471140864.ps2809s79 10.1093/nar/gkz305 10.1074/jbc.AC120.013449 10.1016/0042-6822(91)90071-I 10.1099/vir.0.19424-0 10.1107/S0907444909040074 10.1128/JVI.00733-12 10.1038/nsmb.2523 10.1128/JVI.00713-06 10.1128/JVI.01862-08 10.7554/eLife.28533 10.1002/pro.15 10.1016/bs.aivir.2016.08.008 10.1099/vir.0.031856-0 10.1371/journal.ppat.1008536 10.1128/JVI.03443-13 10.3389/fmed.2020.00295 10.1016/j.str.2005.07.022 10.1107/S2059798319011471 10.1107/S0907444911001314 10.1126/science.1529340 10.1021/bi00415a063 10.1093/jtm/taaa011 10.1038/s41586-020-2008-3 10.1107/S0907444909042073 10.3390/v12060646 10.1080/10408363.2020.1783198 10.1107/S0021889892009944 10.1016/S0168-9525(00)02024-2 10.1038/srep41746 10.1038/s41564-020-0695-z 10.1038/s41579-018-0118-9 10.1107/S0907444909042589 10.1016/j.antiviral.2017.11.001 10.1128/JVI.00705-16 10.1007/s12250-016-3742-4 10.1002/prot.25039 10.1080/10409238.2017.1394265 10.1371/journal.ppat.1007756 10.1107/S0907444906019949 10.1093/nar/18.7.1825 10.1126/science.1218231 10.1107/S0907444903007947 10.1107/S0907444910007493 10.1093/nar/gkq366 10.1107/S0567739478001114 10.1016/j.antiviral.2014.12.015
ContentType	Journal Article
Copyright	Karolina Michalska et al. 2020. COPYRIGHT 2020 International Union of Crystallography 2020. This article is published under https://creativecommons.org/licenses/by/4.0/ (“the License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. Karolina Michalska et al. 2020 2020
Copyright_xml	– notice: Karolina Michalska et al. 2020. – notice: COPYRIGHT 2020 International Union of Crystallography – notice: 2020. This article is published under https://creativecommons.org/licenses/by/4.0/ (“the License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. – notice: Karolina Michalska et al. 2020 2020
CorporateAuthor	Argonne National Lab. (ANL), Argonne, IL (United States)
CorporateAuthor_xml	– name: Argonne National Lab. (ANL), Argonne, IL (United States)
DBID	AAYXX CITATION NPM 7SR 7U5 8BQ 8FD 8FE 8FG ABJCF ABUWG AFKRA AZQEC BENPR BGLVJ CCPQU COVID D1I DWQXO EHMNL HCIFZ JG9 KB. L7M PDBOC PHGZM PHGZT PIMPY PKEHL PQEST PQGLB PQQKQ PQUKI PRINS 7X8 OIOZB OTOTI 5PM DOA
DOI	10.1107/S2052252520009653
DatabaseName	CrossRef PubMed Engineered Materials Abstracts Solid State and Superconductivity Abstracts METADEX Technology Research Database ProQuest SciTech Collection ProQuest Technology Collection Materials Science & Engineering Collection ProQuest Central (Alumni) ProQuest Central UK/Ireland ProQuest Central Essentials - QC ProQuest Central Technology Collection ProQuest One Community College Coronavirus Research Database ProQuest Materials Science Collection ProQuest Central Korea UK & Ireland Database (ProQuest) SciTech Premium Collection Materials Research Database Materials Science Database Advanced Technologies Database with Aerospace Materials Science Collection Proquest Central Premium ProQuest One Academic (New) ProQuest - Publicly Available Content Database ProQuest One Academic Middle East (New) ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Applied & Life Sciences ProQuest One Academic (retired) ProQuest One Academic UKI Edition ProQuest Central China MEDLINE - Academic OSTI.GOV - Hybrid OSTI.GOV PubMed Central (Full Participant titles) DOAJ Directory of Open Access Journals
DatabaseTitle	CrossRef PubMed Publicly Available Content Database Materials Research Database Technology Collection Technology Research Database ProQuest One Academic Middle East (New) ProQuest Central Essentials Materials Science Collection ProQuest Central (Alumni Edition) SciTech Premium Collection ProQuest One Community College ProQuest Central China ProQuest Central ProQuest One Applied & Life Sciences Engineered Materials Abstracts ProQuest Central Korea Materials Science Database ProQuest Central (New) Advanced Technologies Database with Aerospace ProQuest Materials Science Collection ProQuest One Academic Eastern Edition Coronavirus Research Database ProQuest Technology Collection ProQuest SciTech Collection METADEX UK & Ireland Database ProQuest One Academic UKI Edition Materials Science & Engineering Collection Solid State and Superconductivity Abstracts ProQuest One Academic ProQuest One Academic (New) MEDLINE - Academic
DatabaseTitleList	MEDLINE - Academic CrossRef PubMed Publicly Available Content Database
Database_xml	– sequence: 1 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 3 dbid: KB. name: Materials Science Database url: http://search.proquest.com/materialsscijournals sourceTypes: Aggregation Database
DeliveryMethod	fulltext_linktorsrc
Discipline	Engineering
DocumentTitleAlternate	Structure of SARS-CoV-2 ADRP
EISSN	2052-2525
EndPage	824
ExternalDocumentID	oai_doaj_org_article_cb035836f3254f6cb1990635237e5aeb PMC7467174 1774292 A636516473 32939273 10_1107_S2052252520009653
Genre	Journal Article
GrantInformation_xml	– fundername: NIAID NIH HHS grantid: HHSN272201700060C – fundername: National Institute of Allergy and Infectious Diseases grantid: HHSN272201700060C
GroupedDBID	5VS 8FE 8FG AAFWJ AAYXX ABJCF ABUWG ADBBV AENEX AFFHD AFKRA AFPKN ALMA_UNASSIGNED_HOLDINGS AOIJS BCNDV BENPR BGLVJ BPHCQ CCPQU CITATION D1I EBS EHMNL GROUPED_DOAJ H13 HCIFZ HYE IAO ITC KB. KQ8 M48 M~E OK1 PDBOC PGMZT PHGZM PHGZT PIMPY PQGLB PQQKQ PROAC RCJ ROL RPM ZBA NPM 7SR 7U5 8BQ 8FD AZQEC COVID DWQXO JG9 L7M PKEHL PQEST PQUKI PRINS 7X8 3V. OIOZB OTOTI 5PM
ID	FETCH-LOGICAL-c5023-c38ac0a1b844409173dee30dd3edd54fcd8f4eef44a72bf7781d0e5e09baf8ea3
IEDL.DBID	DOA
ISSN	2052-2525
IngestDate	Tue Oct 14 19:06:20 EDT 2025 Tue Nov 04 01:57:59 EST 2025 Thu May 18 22:25:31 EDT 2023 Sun Nov 09 10:38:34 EST 2025 Fri Jul 25 12:03:47 EDT 2025 Tue Nov 11 10:41:23 EST 2025 Tue Nov 04 17:57:22 EST 2025 Mon Jul 21 06:04:58 EDT 2025 Sat Nov 29 01:43:47 EST 2025 Tue Nov 18 21:33:51 EST 2025
IsDoiOpenAccess	true
IsOpenAccess	true
IsPeerReviewed	true
IsScholarly	true
Issue	5
Keywords	COVID-19 SARS-CoV-2 Mac1 crystal structure macrodomain ADP-ribose phosphatase domain Nsp3 ADP-ribosylation ADRP
Language	English
License	Karolina Michalska et al. 2020. This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
LinkModel	DirectLink
MergedId	FETCHMERGED-LOGICAL-c5023-c38ac0a1b844409173dee30dd3edd54fcd8f4eef44a72bf7781d0e5e09baf8ea3
Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 AC02-06CH11357 National Institutes of Health (NIH) - National Institute of Allergy and Infectious Diseases (NIAID) USDOE Office of Science (SC), Biological and Environmental Research (BER) These authors made equal contributions.
ORCID	0000-0003-2535-6209 0000000325356209
OpenAccessLink	https://doaj.org/article/cb035836f3254f6cb1990635237e5aeb
PMID	32939273
PQID	2604483607
PQPubID	2035043
PageCount	11
ParticipantIDs	doaj_primary_oai_doaj_org_article_cb035836f3254f6cb1990635237e5aeb pubmedcentral_primary_oai_pubmedcentral_nih_gov_7467174 osti_scitechconnect_1774292 proquest_miscellaneous_2443885086 proquest_journals_2604483607 gale_infotracmisc_A636516473 gale_infotracacademiconefile_A636516473 pubmed_primary_32939273 crossref_citationtrail_10_1107_S2052252520009653 crossref_primary_10_1107_S2052252520009653
PublicationCentury	2000
PublicationDate	2020-Sep-01
PublicationDateYYYYMMDD	2020-09-01
PublicationDate_xml	– month: 09 year: 2020 text: 2020-Sep-01 day: 01
PublicationDecade	2020
PublicationPlace	England
PublicationPlace_xml	– name: England – name: Chester – name: United States
PublicationTitle	IUCrJ
PublicationTitleAlternate	IUCrJ
PublicationYear	2020
Publisher	International Union of Crystallography
Publisher_xml	– name: International Union of Crystallography
References	Murshudov (lz5040_bb39) 2011; 67 Jankevicius (lz5040_bb24) 2013; 20 Atasheva (lz5040_bb2) 2012; 86 Liebschner (lz5040_bb1) 2019; 75 Hintze (lz5040_bb21) 2016; 84 lz5040_bb10 Thiel (lz5040_bb48) 2003; 84 Báez-Santos (lz5040_bb4) 2015; 115 Wojdyla (lz5040_bb52) 2009; 65 Bogoch (lz5040_bb5) 2020; 27 Minor (lz5040_bb35) 2006; 62 Rack (lz5040_bb43) 2016; 85 Bredenbeek (lz5040_bb6) 1990; 18 Claverie (lz5040_bb9) 2020; 12 Chen (lz5040_bb13) 2010; 66 Cui (lz5040_bb12) 2019; 17 Laskowski (lz5040_bb29) 1993; 26 Fontana (lz5040_bb18) 2017; 6 Pehrson (lz5040_bb41) 1992; 257 Xu (lz5040_bb54) 2009; 83 Munnur (lz5040_bb38) 2019; 47 Malet (lz5040_bb34) 2009; 83 Eckei (lz5040_bb15) 2017; 7 Kuri (lz5040_bb28) 2011; 92 Lei (lz5040_bb32) 2018; 149 Li (lz5040_bb33) 2016; 90 Münnich (lz5040_bb37) 1988; 36 Tang (lz5040_bb47) 2020; 16 Atasheva (lz5040_bb3) 2014; 88 Huynh (lz5040_bb23) 2015; 79 Karplus (lz5040_bb25) 2012; 336 Lee (lz5040_bb30) 1991; 180 Koh (lz5040_bb27) 2020; 7 Moss (lz5040_bb36) 1988; 27 Piotrowski (lz5040_bb42) 2009; 18 Lei (lz5040_bb31) 2016; 31 Padilla (lz5040_bb40) 2003; 59 Cho (lz5040_bb7) 2016; 291 Emsley (lz5040_bb17) 2010; 66 Vagin (lz5040_bb49) 2010; 66 lz5040_bb26 Saikatendu (lz5040_bb45) 2005; 13 Snijder (lz5040_bb46) 2016; 96 Grunewald (lz5040_bb20) 2019; 15 lz5040_bb8 French (lz5040_bb19) 1978; 34 Holm (lz5040_bb22) 2010; 38 Wu (lz5040_bb53) 2020; 579 Virdi (lz5040_bb50) 2020 Winn (lz5040_bb51) 2011; 67 Crawford (lz5040_bb11) 2018; 53 Egloff (lz5040_bb16) 2006; 80 Rice (lz5040_bb44) 2000; 16
References_xml	– volume: 83 start-page: 6534 year: 2009 ident: lz5040_bb34 publication-title: J. Virol. doi: 10.1128/JVI.00189-09 – volume: 67 start-page: 235 year: 2011 ident: lz5040_bb51 publication-title: Acta Cryst. D doi: 10.1107/S0907444910045749 – volume: 85 start-page: 431 year: 2016 ident: lz5040_bb43 publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev-biochem-060815-014935 – volume: 291 start-page: 4894 year: 2016 ident: lz5040_bb7 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M115.700542 – volume: 79 start-page: 2891 year: 2015 ident: lz5040_bb23 publication-title: Curr. Protoc. Protein Sci. doi: 10.1002/0471140864.ps2809s79 – volume: 47 start-page: 5658 year: 2019 ident: lz5040_bb38 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkz305 – ident: lz5040_bb26 doi: 10.1074/jbc.AC120.013449 – volume: 180 start-page: 567 year: 1991 ident: lz5040_bb30 publication-title: Virology doi: 10.1016/0042-6822(91)90071-I – volume: 84 start-page: 2305 year: 2003 ident: lz5040_bb48 publication-title: J. Gen. Virol. doi: 10.1099/vir.0.19424-0 – volume: 65 start-page: 1292 year: 2009 ident: lz5040_bb52 publication-title: Acta Cryst. D doi: 10.1107/S0907444909040074 – volume: 86 start-page: 8147 year: 2012 ident: lz5040_bb2 publication-title: J. Virol. doi: 10.1128/JVI.00733-12 – volume: 20 start-page: 508 year: 2013 ident: lz5040_bb24 publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.2523 – volume: 80 start-page: 8493 year: 2006 ident: lz5040_bb16 publication-title: J. Virol. doi: 10.1128/JVI.00713-06 – volume: 83 start-page: 1083 year: 2009 ident: lz5040_bb54 publication-title: J. Virol. doi: 10.1128/JVI.01862-08 – volume: 6 start-page: e28533 year: 2017 ident: lz5040_bb18 publication-title: eLife doi: 10.7554/eLife.28533 – volume: 18 start-page: 6 year: 2009 ident: lz5040_bb42 publication-title: Protein Sci. doi: 10.1002/pro.15 – volume: 96 start-page: 59 year: 2016 ident: lz5040_bb46 publication-title: Adv. Virus Res. doi: 10.1016/bs.aivir.2016.08.008 – volume: 92 start-page: 1899 year: 2011 ident: lz5040_bb28 publication-title: J. Gen. Virol. doi: 10.1099/vir.0.031856-0 – volume: 16 start-page: e1008536 year: 2020 ident: lz5040_bb47 publication-title: PLoS Pathog. doi: 10.1371/journal.ppat.1008536 – volume: 88 start-page: 2116 year: 2014 ident: lz5040_bb3 publication-title: J. Virol. doi: 10.1128/JVI.03443-13 – volume: 7 start-page: 295 year: 2020 ident: lz5040_bb27 publication-title: Front. Med. (Lausanne) doi: 10.3389/fmed.2020.00295 – volume: 13 start-page: 1665 year: 2005 ident: lz5040_bb45 publication-title: Structure doi: 10.1016/j.str.2005.07.022 – volume: 75 start-page: 861 year: 2019 ident: lz5040_bb1 publication-title: Acta Cryst. D doi: 10.1107/S2059798319011471 – volume: 67 start-page: 355 year: 2011 ident: lz5040_bb39 publication-title: Acta Cryst. D doi: 10.1107/S0907444911001314 – volume: 257 start-page: 1398 year: 1992 ident: lz5040_bb41 publication-title: Science doi: 10.1126/science.1529340 – volume: 27 start-page: 5819 year: 1988 ident: lz5040_bb36 publication-title: Biochemistry doi: 10.1021/bi00415a063 – volume: 27 start-page: taaa011 year: 2020 ident: lz5040_bb5 publication-title: J. Travel Med. doi: 10.1093/jtm/taaa011 – start-page: 20200706190413 year: 2020 ident: lz5040_bb50 publication-title: bioRxiv – volume: 579 start-page: 265 year: 2020 ident: lz5040_bb53 publication-title: Nature doi: 10.1038/s41586-020-2008-3 – volume: 66 start-page: 12 year: 2010 ident: lz5040_bb13 publication-title: Acta Cryst. D doi: 10.1107/S0907444909042073 – volume: 12 start-page: 646 year: 2020 ident: lz5040_bb9 publication-title: Viruses doi: 10.3390/v12060646 – ident: lz5040_bb8 doi: 10.1080/10408363.2020.1783198 – volume: 26 start-page: 283 year: 1993 ident: lz5040_bb29 publication-title: J. Appl. Cryst. doi: 10.1107/S0021889892009944 – volume: 16 start-page: 276 year: 2000 ident: lz5040_bb44 publication-title: Trends Genet. doi: 10.1016/S0168-9525(00)02024-2 – volume: 7 start-page: 41746 year: 2017 ident: lz5040_bb15 publication-title: Sci. Rep. doi: 10.1038/srep41746 – ident: lz5040_bb10 doi: 10.1038/s41564-020-0695-z – volume: 17 start-page: 181 year: 2019 ident: lz5040_bb12 publication-title: Nat. Rev. Microbiol. doi: 10.1038/s41579-018-0118-9 – volume: 66 start-page: 22 year: 2010 ident: lz5040_bb49 publication-title: Acta Cryst. D doi: 10.1107/S0907444909042589 – volume: 149 start-page: 58 year: 2018 ident: lz5040_bb32 publication-title: Antiviral Res. doi: 10.1016/j.antiviral.2017.11.001 – volume: 90 start-page: 8478 year: 2016 ident: lz5040_bb33 publication-title: J. Virol. doi: 10.1128/JVI.00705-16 – volume: 31 start-page: 288 year: 2016 ident: lz5040_bb31 publication-title: Virol. Sin. doi: 10.1007/s12250-016-3742-4 – volume: 84 start-page: 1177 year: 2016 ident: lz5040_bb21 publication-title: Proteins doi: 10.1002/prot.25039 – volume: 53 start-page: 64 year: 2018 ident: lz5040_bb11 publication-title: Crit. Rev. Biochem. Mol. Biol. doi: 10.1080/10409238.2017.1394265 – volume: 15 start-page: e1007756 year: 2019 ident: lz5040_bb20 publication-title: PLoS Pathog. doi: 10.1371/journal.ppat.1007756 – volume: 62 start-page: 859 year: 2006 ident: lz5040_bb35 publication-title: Acta Cryst. D doi: 10.1107/S0907444906019949 – volume: 18 start-page: 1825 year: 1990 ident: lz5040_bb6 publication-title: Nucleic Acids Res. doi: 10.1093/nar/18.7.1825 – volume: 336 start-page: 1030 year: 2012 ident: lz5040_bb25 publication-title: Science doi: 10.1126/science.1218231 – volume: 59 start-page: 1124 year: 2003 ident: lz5040_bb40 publication-title: Acta Cryst. D doi: 10.1107/S0907444903007947 – volume: 66 start-page: 486 year: 2010 ident: lz5040_bb17 publication-title: Acta Cryst. D doi: 10.1107/S0907444910007493 – volume: 38 start-page: W545 year: 2010 ident: lz5040_bb22 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkq366 – volume: 34 start-page: 517 year: 1978 ident: lz5040_bb19 publication-title: Acta Cryst. A doi: 10.1107/S0567739478001114 – volume: 36 start-page: 109 year: 1988 ident: lz5040_bb37 publication-title: Ther. Hung. – volume: 115 start-page: 21 year: 2015 ident: lz5040_bb4 publication-title: Antiviral Res. doi: 10.1016/j.antiviral.2014.12.015
SSID	ssj0001125741
Score	2.4906285
Snippet	Among 15 nonstructural proteins (Nsps), the newly emerging Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) encodes a large, multidomain Nsp3. One... High-resolution crystal structures of the ADP-ribose phosphatase domain (ADRP; also known as the macrodomain) from SARS-CoV-2 with multiple ligands illustrate...
SourceID	doaj pubmedcentral osti proquest gale pubmed crossref
SourceType	Open Website Open Access Repository Aggregation Database Index Database Enrichment Source
StartPage	814
SubjectTerms	ADP-ribose phosphatase domain ADP-ribosylation ADRP BASIC BIOLOGICAL SCIENCES Coordination compounds Coronaviruses COVID-19 Crystal structure Enzymes Health aspects Homology Ligands Mac1 macrodomain Monosaccharides Nsp3 Phosphatase Phosphatases Proteins Research Papers Ribose RNA SARS-CoV-2 Severe acute respiratory syndrome Severe acute respiratory syndrome coronavirus 2 Viral diseases Water chemistry
SummonAdditionalLinks	– databaseName: Materials Science Database dbid: KB. link: http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3db9MwELeg8AAPfH-UDWQkJCSkMNd24oQX1A0mJKRpooD2hOXPtVIVl6ZD8N9zl6bdAmgvvMZOYufOd7-zL78j5IXiRXQ585mzEKtKE1VmFGOZw4RK612w0rfFJtTRUXlyUh13G25Nl1a5sYmtofbJ4R75HuBuiCREwdTbxfcMq0bh6WpXQuMquYYsCVi64eP-6_M9FvDe4DG7w0wIdPYmnAHgyDmSDSHviei5o5a1f2ubBwkW2b-A55_5kxcc0uHt_53KHXKrg6J0vNadu-RKqO-RmxcICu-TbwfLXwAf53RNM3sGsTlNkU7GnybZQfqacTp-d5wtZzY1gS6mqVlMzQr84huKv61QAJfULBJFYExXic5np6b2tE1jDz9D84B8OXz_-eBD1lVkyECeXGROlMYxM7KllBAYjpTwIQjmvQje5zI6X0YZQpTSKG6jUoCGWcgDq6yJZTDiIRnUqQ6PCZU2507ZWHmkuI-gKmUhweL4oJyovBsSthGMdh1dOVbNmOs2bGFK_yXLIXm1vWWx5uq4rPM-SnvbEWm22wtpeaq7VathVCIHSUUBcXQsnB2B8waIxoUKuQl2SF6irmg0BjA4Z7p_GmCKSKulx4UocmRsg9ft9nrCIna95h3UNg2wB7l7HSY5uZUeATjnFYebN4qkOxPT6HMtGpLn22Z8LqbN1SGdQR8pRVkCBi-G5NFaZ7cTFgD0Ko6vVj1t7n2Rfks9m7YE5FiiBiLZJ5cPa4fc4Lg50Sbk7ZIBKGp4Sq67H6tZs3zWrtTfHbdD7w priority: 102 providerName: ProQuest
Title	Crystal structures of SARS-CoV-2 ADP-ribose phosphatase: from the apo form to ligand complexes
URI	https://www.ncbi.nlm.nih.gov/pubmed/32939273 https://www.proquest.com/docview/2604483607 https://www.proquest.com/docview/2443885086 https://www.osti.gov/servlets/purl/1774292 https://pubmed.ncbi.nlm.nih.gov/PMC7467174 https://doaj.org/article/cb035836f3254f6cb1990635237e5aeb
Volume	7
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
journalDatabaseRights	– providerCode: PRVAON databaseName: DOAJ Directory of Open Access Journals customDbUrl: eissn: 2052-2525 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0001125741 issn: 2052-2525 databaseCode: DOA dateStart: 20140101 isFulltext: true titleUrlDefault: https://www.doaj.org/ providerName: Directory of Open Access Journals – providerCode: PRVHPJ databaseName: ROAD: Directory of Open Access Scholarly Resources customDbUrl: eissn: 2052-2525 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0001125741 issn: 2052-2525 databaseCode: M~E dateStart: 20140101 isFulltext: true titleUrlDefault: https://road.issn.org providerName: ISSN International Centre – providerCode: PRVPQU databaseName: Materials Science Database customDbUrl: eissn: 2052-2525 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0001125741 issn: 2052-2525 databaseCode: KB. dateStart: 20140101 isFulltext: true titleUrlDefault: http://search.proquest.com/materialsscijournals providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest - Publicly Available Content Database customDbUrl: eissn: 2052-2525 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0001125741 issn: 2052-2525 databaseCode: PIMPY dateStart: 20140101 isFulltext: true titleUrlDefault: http://search.proquest.com/publiccontent providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Central customDbUrl: eissn: 2052-2525 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0001125741 issn: 2052-2525 databaseCode: BENPR dateStart: 20140101 isFulltext: true titleUrlDefault: https://www.proquest.com/central providerName: ProQuest – providerCode: PRVPQU databaseName: UK & Ireland Database (ProQuest) customDbUrl: eissn: 2052-2525 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0001125741 issn: 2052-2525 databaseCode: EHMNL dateStart: 20140101 isFulltext: true titleUrlDefault: https://search.proquest.com/ukireland providerName: ProQuest
link	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lj9MwELagcIAD4k3ZpTISEhJSWMd24oRbW3YFQlTVFlC5YDl-0EpVUrVdBP-emSRbNYDgwiUH23l4Zjz-Jpl8Q8gzxdNgE-YiW0CsKk1QkVGMRRYTKgtnfSFdXWxCTSbZfJ5PD0p9YU5YQw_cCO4EriGSTKRBQCgTUlvE4D9hl-RC-cT4Ar0voJ6DYKp-uwL7tqrLVnKW8IgnPGk_aUK4czLDRmzjNYRPRGdTqrn79x66V8FS-xP8_DWL8mBbOrtNbrV4kg6bedwhV3x5l9w8YBm8R76MNz8AA65owxV7AQE2rQKdDc9n0bj6FHE6fD2NNsui2nq6XlTb9cLsYHN7RfHfEwoIkZp1RRHd0l1FV8uvpnS0zkX33_32Pvl4dvph_CZqyypEoBQuIisyY5mJi0xKiO5iJZz3gjknvHMgY-uyIL0PUhrFi6AUQFrmE8_ywoTMG_GA9Mqq9I8IlUXCrSpC7pCnPoCuslSC23BeWZE72yfsUq7atpzjWPpipevYgyn9myr65MX-lHVDuPG3wSNU1n4gcmXXDWBBurUg_S8L6pPnqGqNKxoezpr2xwSYInJj6WEq0gRp1-B2x52RsBJtp_sIjUUDdkECXouZSnanY0DYPOdw8qUN6dZPbDVEkxAfi5SpPnm678brYu5b6asLGCOlyDIA0mmfPGxMbj9hAWgt53hr1THGjkS6PeVyUbOIY50ZCEcf_w8RHpEbcY4VjPDV1DHpgTn7J-S6_bZbbjcDclXNswG5NjqdTM8H9UKF47vRS2ibvn0__fwTCwA8UQ
linkProvider	Directory of Open Access Journals
linkToHtml	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1db9MwFLVGhwQ88P1RNsBIICSkaKntxAkSmkrHtGpbVdENjReMYztrpSopTQfsT_Ebd2-adgugve2B19pJ7PTc63Od63MJeSVZmJrAt55JIFYVOpWelr7vGUyoTKxxibBlsQnZ60VHR3F_hfxenIXBtMqFTywdtc0N7pFvAO-GSIKHvtycfPewahR-XV2U0JjDYted_oSQrXjf3YL_9zVj2x8POjteVVXAgzEx7hkeaePrVhIJAcFNS3LrHPet5c7aQKTGRqlwLhVCS5akUgKj813g_DjRaeQ0h_teI6sCwB41yGq_u9__cr6rA3wB1ujq8ymEVhsD5gPFCRjKG6HSCq8tgGWdgOVq0MjBrP9Fdf_M2LywBG7f-d9e3l1yuyLbtD23jntkxWX3ya0LEowPyNfO9BQI8pjOhXRPpq6geUoH7U8Dr5N_9hhtb_W96SjJC0cnw7yYDPUMVv53FA_mUKDPVE9yitSfznI6Hh3rzNIyUd_9csVDcnglE3xEGlmeuSeEiiRgRiZpbFHEPwVjiEIBPtU6aXhsTZP4CyAoUwmyY12QsSoDM1-qv7DTJG-Xl0zmaiSXdf6A6Fp2RCHx8od8eqwqv6RgVDwAZKScwexCk7SAngAJZVy6QLukSd4gNhW6Oxic0dWpDZgiCoepdsjDADXp4HHrtZ7gpkyteQ3RrYDYoTqxwTQuM1MtCD9YzODiBXBV5UQLdY7aJnm5bMb7YmJg5vIT6CMEjyKIMsImeTy3keWEOVDZmOGjZc16am-k3pKNhqXEOhbhgVj96eXDekFu7Bzs76m9bm93jdxkuBVTph-ukwaA1j0j182P2aiYPq_8BCXfrtq6zgDenqVa
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=Crystal+structures+of+SARS-CoV-2+ADP-ribose+phosphatase%3A+from+the+apo+form+to+ligand+complexes&rft.jtitle=IUCrJ&rft.au=Michalska%2C+Karolina&rft.au=Kim%2C+Youngchang&rft.au=Jedrzejczak%2C+Robert&rft.au=Maltseva%2C+Natalia+I&rft.date=2020-09-01&rft.issn=2052-2525&rft.eissn=2052-2525&rft.volume=7&rft.issue=Pt+5&rft.spage=814&rft_id=info:doi/10.1107%2FS2052252520009653&rft.externalDBID=NO_FULL_TEXT
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2052-2525&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2052-2525&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2052-2525&client=summon