Structures of the Middle East respiratory syndrome coronavirus 3C-like protease reveal insights into substrate specificity.
Identifieur interne : 000E23 ( PubMed/Corpus ); précédent : 000E22; suivant : 000E24Structures of the Middle East respiratory syndrome coronavirus 3C-like protease reveal insights into substrate specificity.
Auteurs : Danielle Needle ; George T. Lountos ; David S. WaughSource :
- Acta crystallographica. Section D, Biological crystallography [ 1399-0047 ] ; 2015.
English descriptors
- KwdEn :
- Amino Acid Sequence, Antiviral Agents (pharmacology), Catalytic Domain, Crystallography, X-Ray, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (metabolism), Enzyme Inhibitors (pharmacology), Humans, Middle East Respiratory Syndrome Coronavirus (enzymology), Models, Molecular, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid, Substrate Specificity.
- MESH :
- chemical , chemistry : Cysteine Endopeptidases.
- chemical , metabolism : Cysteine Endopeptidases.
- chemical , pharmacology : Antiviral Agents, Enzyme Inhibitors.
- enzymology : Middle East Respiratory Syndrome Coronavirus.
- Amino Acid Sequence, Catalytic Domain, Crystallography, X-Ray, Humans, Models, Molecular, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid, Substrate Specificity.
Abstract
Middle East respiratory syndrome coronavirus (MERS-CoV) is a highly pathogenic virus that causes severe respiratory illness accompanied by multi-organ dysfunction, resulting in a case fatality rate of approximately 40%. As found in other coronaviruses, the majority of the positive-stranded RNA MERS-CoV genome is translated into two polyproteins, one created by a ribosomal frameshift, that are cleaved at three sites by a papain-like protease and at 11 sites by a 3C-like protease (3 CL(pro)). Since 3 CL(pro) is essential for viral replication, it is a leading candidate for therapeutic intervention. To accelerate the development of 3 CL(pro) inhibitors, three crystal structures of a catalytically inactive variant (C148A) of the MERS-CoV 3 CL(pro) enzyme were determined. The aim was to co-crystallize the inactive enzyme with a peptide substrate. Fortuitously, however, in two of the structures the C-terminus of one protomer is bound in the active site of a neighboring molecule, providing a snapshot of an enzyme-product complex. In the third structure, two of the three protomers in the asymmetric unit form a homodimer similar to that of SARS-CoV 3 CL(pro); however, the third protomer adopts a radically different conformation that is likely to correspond to a crystallographic monomer, indicative of substantial structural plasticity in the enzyme. The results presented here provide a foundation for the structure-based design of small-molecule inhibitors of the MERS-CoV 3 CL(pro) enzyme.
DOI: 10.1107/S1399004715003521
PubMed: 25945576
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structures of the Middle East respiratory syndrome coronavirus 3C-like protease reveal insights into substrate specificity.</title><author><name sortKey="Needle, Danielle" sort="Needle, Danielle" uniqKey="Needle D" first="Danielle" last="Needle">Danielle Needle</name><affiliation><nlm:affiliation>Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, Maryland, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Lountos, George T" sort="Lountos, George T" uniqKey="Lountos G" first="George T" last="Lountos">George T. Lountos</name><affiliation><nlm:affiliation>Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, Maryland, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Waugh, David S" sort="Waugh, David S" uniqKey="Waugh D" first="David S" last="Waugh">David S. Waugh</name><affiliation><nlm:affiliation>Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, Maryland, USA.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:25945576</idno><idno type="pmid">25945576</idno><idno type="doi">10.1107/S1399004715003521</idno><idno type="wicri:Area/PubMed/Corpus">000E23</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000E23</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Structures of the Middle East respiratory syndrome coronavirus 3C-like protease reveal insights into substrate specificity.</title><author><name sortKey="Needle, Danielle" sort="Needle, Danielle" uniqKey="Needle D" first="Danielle" last="Needle">Danielle Needle</name><affiliation><nlm:affiliation>Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, Maryland, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Lountos, George T" sort="Lountos, George T" uniqKey="Lountos G" first="George T" last="Lountos">George T. Lountos</name><affiliation><nlm:affiliation>Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, Maryland, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Waugh, David S" sort="Waugh, David S" uniqKey="Waugh D" first="David S" last="Waugh">David S. Waugh</name><affiliation><nlm:affiliation>Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, Maryland, USA.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Acta crystallographica. 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As found in other coronaviruses, the majority of the positive-stranded RNA MERS-CoV genome is translated into two polyproteins, one created by a ribosomal frameshift, that are cleaved at three sites by a papain-like protease and at 11 sites by a 3C-like protease (3 CL(pro)). Since 3 CL(pro) is essential for viral replication, it is a leading candidate for therapeutic intervention. To accelerate the development of 3 CL(pro) inhibitors, three crystal structures of a catalytically inactive variant (C148A) of the MERS-CoV 3 CL(pro) enzyme were determined. The aim was to co-crystallize the inactive enzyme with a peptide substrate. Fortuitously, however, in two of the structures the C-terminus of one protomer is bound in the active site of a neighboring molecule, providing a snapshot of an enzyme-product complex. In the third structure, two of the three protomers in the asymmetric unit form a homodimer similar to that of SARS-CoV 3 CL(pro); however, the third protomer adopts a radically different conformation that is likely to correspond to a crystallographic monomer, indicative of substantial structural plasticity in the enzyme. The results presented here provide a foundation for the structure-based design of small-molecule inhibitors of the MERS-CoV 3 CL(pro) enzyme.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25945576</PMID><DateCompleted><Year>2016</Year><Month>02</Month><Day>04</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>19</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1399-0047</ISSN><JournalIssue CitedMedium="Internet"><Volume>71</Volume><Issue>Pt 5</Issue><PubDate><Year>2015</Year><Month>May</Month></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Biological crystallography</Title><ISOAbbreviation>Acta Crystallogr. D Biol. Crystallogr.</ISOAbbreviation></Journal><ArticleTitle>Structures of the Middle East respiratory syndrome coronavirus 3C-like protease reveal insights into substrate specificity.</ArticleTitle><Pagination><MedlinePgn>1102-11</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1107/S1399004715003521</ELocationID><Abstract><AbstractText>Middle East respiratory syndrome coronavirus (MERS-CoV) is a highly pathogenic virus that causes severe respiratory illness accompanied by multi-organ dysfunction, resulting in a case fatality rate of approximately 40%. As found in other coronaviruses, the majority of the positive-stranded RNA MERS-CoV genome is translated into two polyproteins, one created by a ribosomal frameshift, that are cleaved at three sites by a papain-like protease and at 11 sites by a 3C-like protease (3 CL(pro)). Since 3 CL(pro) is essential for viral replication, it is a leading candidate for therapeutic intervention. To accelerate the development of 3 CL(pro) inhibitors, three crystal structures of a catalytically inactive variant (C148A) of the MERS-CoV 3 CL(pro) enzyme were determined. The aim was to co-crystallize the inactive enzyme with a peptide substrate. Fortuitously, however, in two of the structures the C-terminus of one protomer is bound in the active site of a neighboring molecule, providing a snapshot of an enzyme-product complex. In the third structure, two of the three protomers in the asymmetric unit form a homodimer similar to that of SARS-CoV 3 CL(pro); however, the third protomer adopts a radically different conformation that is likely to correspond to a crystallographic monomer, indicative of substantial structural plasticity in the enzyme. The results presented here provide a foundation for the structure-based design of small-molecule inhibitors of the MERS-CoV 3 CL(pro) enzyme.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Needle</LastName><ForeName>Danielle</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, Maryland, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lountos</LastName><ForeName>George T</ForeName><Initials>GT</Initials><AffiliationInfo><Affiliation>Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, Maryland, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Waugh</LastName><ForeName>David S</ForeName><Initials>DS</Initials><AffiliationInfo><Affiliation>Macromolecular Crystallography Laboratory, Center for Cancer 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