Structure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer.
Identifieur interne : 002323 ( PubMed/Corpus ); précédent : 002322; suivant : 002324Structure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer.
Auteurs : Ting Xu ; Amy Ooi ; Hooi Chen Lee ; Rupert Wilmouth ; Ding Xiang Liu ; Julien LescarSource :
- Acta crystallographica. Section F, Structural biology and crystallization communications [ 1744-3091 ] ; 2005.
English descriptors
- KwdEn :
- Binding Sites, Catalysis, Catalytic Domain, Crystallography, X-Ray, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (metabolism), DNA Fragmentation, Dimerization, Enzyme Inhibitors (chemistry), Hydrogen-Ion Concentration, Models, Molecular, Models, Statistical, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, SARS Virus (enzymology), Viral Proteins (chemistry), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Cysteine Endopeptidases, Enzyme Inhibitors, Viral Proteins.
- chemical , metabolism : Cysteine Endopeptidases, Viral Proteins.
- enzymology : SARS Virus.
- Binding Sites, Catalysis, Catalytic Domain, Crystallography, X-Ray, DNA Fragmentation, Dimerization, Hydrogen-Ion Concentration, Models, Molecular, Models, Statistical, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary.
Abstract
The 34 kDa main proteinase (Mpro) from the severe acute respiratory syndrome coronavirus (SARS-CoV) plays an important role in the virus life cycle through the specific processing of viral polyproteins. As such, SARS-CoV Mpro is a key target for the identification of specific inhibitors directed against the SARS virus. With a view to facilitating the development of such compounds, crystals were obtained of the enzyme at pH 6.5 in the orthorhombic space group P2(1)2(1)2 that diffract to a resolution of 1.9 A. These crystals contain one monomer per asymmetric unit and the biologically active dimer is generated via the crystallographic twofold axis. The conformation of the catalytic site indicates that the enzyme is active in the crystalline form and thus suitable for structure-based inhibition studies.
DOI: 10.1107/S1744309105033257
PubMed: 16511208
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pubmed:16511208Le document en format XML
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Section F, Structural biology and crystallization communications</title><idno type="eISSN">1744-3091</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites</term><term>Catalysis</term><term>Catalytic Domain</term><term>Crystallography, X-Ray</term><term>Cysteine Endopeptidases (chemistry)</term><term>Cysteine Endopeptidases (metabolism)</term><term>DNA Fragmentation</term><term>Dimerization</term><term>Enzyme Inhibitors (chemistry)</term><term>Hydrogen-Ion Concentration</term><term>Models, Molecular</term><term>Models, Statistical</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>SARS Virus (enzymology)</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Enzyme Inhibitors</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Catalysis</term><term>Catalytic Domain</term><term>Crystallography, X-Ray</term><term>DNA Fragmentation</term><term>Dimerization</term><term>Hydrogen-Ion Concentration</term><term>Models, Molecular</term><term>Models, Statistical</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The 34 kDa main proteinase (Mpro) from the severe acute respiratory syndrome coronavirus (SARS-CoV) plays an important role in the virus life cycle through the specific processing of viral polyproteins. As such, SARS-CoV Mpro is a key target for the identification of specific inhibitors directed against the SARS virus. With a view to facilitating the development of such compounds, crystals were obtained of the enzyme at pH 6.5 in the orthorhombic space group P2(1)2(1)2 that diffract to a resolution of 1.9 A. These crystals contain one monomer per asymmetric unit and the biologically active dimer is generated via the crystallographic twofold axis. The conformation of the catalytic site indicates that the enzyme is active in the crystalline form and thus suitable for structure-based inhibition studies.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16511208</PMID><DateCompleted><Year>2006</Year><Month>06</Month><Day>02</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1744-3091</ISSN><JournalIssue CitedMedium="Internet"><Volume>61</Volume><Issue>Pt 11</Issue><PubDate><Year>2005</Year><Month>Nov</Month><Day>01</Day></PubDate></JournalIssue><Title>Acta crystallographica. Section F, Structural biology and crystallization communications</Title><ISOAbbreviation>Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.</ISOAbbreviation></Journal><ArticleTitle>Structure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer.</ArticleTitle><Pagination><MedlinePgn>964-6</MedlinePgn></Pagination><Abstract><AbstractText>The 34 kDa main proteinase (Mpro) from the severe acute respiratory syndrome coronavirus (SARS-CoV) plays an important role in the virus life cycle through the specific processing of viral polyproteins. As such, SARS-CoV Mpro is a key target for the identification of specific inhibitors directed against the SARS virus. With a view to facilitating the development of such compounds, crystals were obtained of the enzyme at pH 6.5 in the orthorhombic space group P2(1)2(1)2 that diffract to a resolution of 1.9 A. These crystals contain one monomer per asymmetric unit and the biologically active dimer is generated via the crystallographic twofold axis. The conformation of the catalytic site indicates that the enzyme is active in the crystalline form and thus suitable for structure-based inhibition studies.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Xu</LastName><ForeName>Ting</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, Singapore 637551, Singapore.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ooi</LastName><ForeName>Amy</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Hooi Chen</ForeName><Initials>HC</Initials></Author><Author ValidYN="Y"><LastName>Wilmouth</LastName><ForeName>Rupert</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Ding Xiang</ForeName><Initials>DX</Initials></Author><Author ValidYN="Y"><LastName>Lescar</LastName><ForeName>Julien</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>10</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Acta Crystallogr Sect F Struct Biol Cryst Commun</MedlineTA><NlmUniqueID>101226117</NlmUniqueID><ISSNLinking>1744-3091</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="C099456">3C-like proteinase, 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