Crystal structures of the main peptidase from the SARS coronavirus inhibited by a substrate-like aza-peptide epoxide.
Identifieur interne : 001201 ( Ncbi/Merge ); précédent : 001200; suivant : 001202Crystal structures of the main peptidase from the SARS coronavirus inhibited by a substrate-like aza-peptide epoxide.
Auteurs : Ting-Wai Lee [Canada] ; Maia M. Cherney ; Carly Huitema ; Jie Liu ; Karen Ellis James ; James C. Powers ; Lindsay D. Eltis ; Michael N G. JamesSource :
- Journal of molecular biology [ 0022-2836 ] ; 2005.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Cysteine Endopeptidases, Epoxy Compounds, Peptides, Protease Inhibitors.
- chemistry : SARS Virus.
- Binding Sites, Catalysis, Crystallography, X-Ray, Hydrogen-Ion Concentration, Molecular Structure.
Abstract
The main peptidase (M(pro)) from the coronavirus (CoV) causing severe acute respiratory syndrome (SARS) is one of the most attractive molecular targets for the development of anti-SARS agents. We report the irreversible inhibition of SARS-CoV M(pro) by an aza-peptide epoxide (APE; k(inact)/K(i) = 1900(+/-400) M(-1) s(-1)). The crystal structures of the M(pro):APE complex in the space groups C2 and P2(1)2(1)2(1) revealed the formation of a covalent bond between the catalytic Cys145 S(gamma) atom of the peptidase and the epoxide C3 atom of the inhibitor, substantiating the mode of action of this class of cysteine-peptidase inhibitors. The aza-peptide component of APE binds in the substrate-binding regions of M(pro) in a substrate-like manner, with excellent structural and chemical complementarity. In addition, the crystal structure of unbound M(pro) in the space group C2 revealed that the "N-fingers" (N-terminal residues 1 to 7) of both protomers of M(pro) are well defined and the substrate-binding regions of both protomers are in the catalytically competent conformation at the crystallization pH of 6.5, contrary to the previously determined crystal structures of unbound M(pro) in the space group P2(1).
DOI: 10.1016/j.jmb.2005.09.004
PubMed: 16219322
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Cherney</name></author><author><name sortKey="Huitema, Carly" sort="Huitema, Carly" uniqKey="Huitema C" first="Carly" last="Huitema">Carly Huitema</name></author><author><name sortKey="Liu, Jie" sort="Liu, Jie" uniqKey="Liu J" first="Jie" last="Liu">Jie Liu</name></author><author><name sortKey="James, Karen Ellis" sort="James, Karen Ellis" uniqKey="James K" first="Karen Ellis" last="James">Karen Ellis James</name></author><author><name sortKey="Powers, James C" sort="Powers, James C" uniqKey="Powers J" first="James C" last="Powers">James C. Powers</name></author><author><name sortKey="Eltis, Lindsay D" sort="Eltis, Lindsay D" uniqKey="Eltis L" first="Lindsay D" last="Eltis">Lindsay D. Eltis</name></author><author><name sortKey="James, Michael N G" sort="James, Michael N G" uniqKey="James M" first="Michael N G" last="James">Michael N G. James</name></author></analytic><series><title level="j">Journal of molecular biology</title><idno type="ISSN">0022-2836</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>Crystallography, X-Ray</term><term>Cysteine Endopeptidases (chemistry)</term><term>Epoxy Compounds (chemistry)</term><term>Hydrogen-Ion Concentration</term><term>Molecular Structure</term><term>Peptides (chemistry)</term><term>Protease Inhibitors (chemistry)</term><term>SARS Virus (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Catalyse</term><term>Composés époxy ()</term><term>Concentration en ions d'hydrogène</term><term>Cristallographie aux rayons X</term><term>Cysteine endopeptidases ()</term><term>Inhibiteurs de protéases ()</term><term>Peptides ()</term><term>Sites de fixation</term><term>Structure moléculaire</term><term>Virus du SRAS ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Epoxy Compounds</term><term>Peptides</term><term>Protease Inhibitors</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Catalysis</term><term>Crystallography, X-Ray</term><term>Hydrogen-Ion Concentration</term><term>Molecular Structure</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Composés époxy</term><term>Concentration en ions d'hydrogène</term><term>Cristallographie aux rayons X</term><term>Cysteine endopeptidases</term><term>Inhibiteurs de protéases</term><term>Peptides</term><term>Sites de fixation</term><term>Structure moléculaire</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The main peptidase (M(pro)) from the coronavirus (CoV) causing severe acute respiratory syndrome (SARS) is one of the most attractive molecular targets for the development of anti-SARS agents. We report the irreversible inhibition of SARS-CoV M(pro) by an aza-peptide epoxide (APE; k(inact)/K(i) = 1900(+/-400) M(-1) s(-1)). The crystal structures of the M(pro):APE complex in the space groups C2 and P2(1)2(1)2(1) revealed the formation of a covalent bond between the catalytic Cys145 S(gamma) atom of the peptidase and the epoxide C3 atom of the inhibitor, substantiating the mode of action of this class of cysteine-peptidase inhibitors. The aza-peptide component of APE binds in the substrate-binding regions of M(pro) in a substrate-like manner, with excellent structural and chemical complementarity. In addition, the crystal structure of unbound M(pro) in the space group C2 revealed that the "N-fingers" (N-terminal residues 1 to 7) of both protomers of M(pro) are well defined and the substrate-binding regions of both protomers are in the catalytically competent conformation at the crystallization pH of 6.5, contrary to the previously determined crystal structures of unbound M(pro) in the space group P2(1).</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16219322</PMID><DateCompleted><Year>2005</Year><Month>12</Month><Day>21</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0022-2836</ISSN><JournalIssue CitedMedium="Print"><Volume>353</Volume><Issue>5</Issue><PubDate><Year>2005</Year><Month>Nov</Month><Day>11</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J. Mol. Biol.</ISOAbbreviation></Journal><ArticleTitle>Crystal structures of the main peptidase from the SARS coronavirus inhibited by a substrate-like aza-peptide epoxide.</ArticleTitle><Pagination><MedlinePgn>1137-51</MedlinePgn></Pagination><Abstract><AbstractText>The main peptidase (M(pro)) from the coronavirus (CoV) causing severe acute respiratory syndrome (SARS) is one of the most attractive molecular targets for the development of anti-SARS agents. We report the irreversible inhibition of SARS-CoV M(pro) by an aza-peptide epoxide (APE; k(inact)/K(i) = 1900(+/-400) M(-1) s(-1)). The crystal structures of the M(pro):APE complex in the space groups C2 and P2(1)2(1)2(1) revealed the formation of a covalent bond between the catalytic Cys145 S(gamma) atom of the peptidase and the epoxide C3 atom of the inhibitor, substantiating the mode of action of this class of cysteine-peptidase inhibitors. The aza-peptide component of APE binds in the substrate-binding regions of M(pro) in a substrate-like manner, with excellent structural and chemical complementarity. In addition, the crystal structure of unbound M(pro) in the space group C2 revealed that the "N-fingers" (N-terminal residues 1 to 7) of both protomers of M(pro) are well defined and the substrate-binding regions of both protomers are in the catalytically competent conformation at the crystallization pH of 6.5, contrary to the previously determined crystal structures of unbound M(pro) in the space group P2(1).</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Ting-Wai</ForeName><Initials>TW</Initials><AffiliationInfo><Affiliation>Canadian Institute of Health Research Group in Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton, Alta., Canada T6G 2H7.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cherney</LastName><ForeName>Maia M</ForeName><Initials>MM</Initials></Author><Author ValidYN="Y"><LastName>Huitema</LastName><ForeName>Carly</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Jie</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>James</LastName><ForeName>Karen Ellis</ForeName><Initials>KE</Initials></Author><Author ValidYN="Y"><LastName>Powers</LastName><ForeName>James C</ForeName><Initials>JC</Initials></Author><Author ValidYN="Y"><LastName>Eltis</LastName><ForeName>Lindsay D</ForeName><Initials>LD</Initials></Author><Author ValidYN="Y"><LastName>James</LastName><ForeName>Michael N G</ForeName><Initials>MN</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>2A5A</AccessionNumber><AccessionNumber>2A5I</AccessionNumber><AccessionNumber>2A5K</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal 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PubStatus="pubmed"><Year>2005</Year><Month>10</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>12</Month><Day>22</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>10</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16219322</ArticleId><ArticleId IdType="pii">S0022-2836(05)01057-0</ArticleId><ArticleId IdType="doi">10.1016/j.jmb.2005.09.004</ArticleId><ArticleId IdType="pmc">PMC7094542</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Anal Biochem. 1999 Feb 15;267(2):331-5</Citation><ArticleIdList><ArticleId IdType="pubmed">10036138</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biol Chem. 2001 May;382(5):727-33</Citation><ArticleIdList><ArticleId IdType="pubmed">11517925</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochim Biophys Acta. 1987 Apr 30;912(3):408-16</Citation><ArticleIdList><ArticleId IdType="pubmed">3567209</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biochem. 2000 Apr;127(4):635-43</Citation><ArticleIdList><ArticleId IdType="pubmed">10739956</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2004 Jan 16;279(3):1637-42</Citation><ArticleIdList><ArticleId IdType="pubmed">14561748</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Pathol. 2003 Jul;200(3):282-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12845623</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Methods Enzymol. 1997;276:307-26</Citation><ArticleIdList><ArticleId IdType="pubmed">27754618</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2004 Jun 4;279(23):24765-73</Citation><ArticleIdList><ArticleId IdType="pubmed">15037623</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2004 May 4;43(17):4906-12</Citation><ArticleIdList><ArticleId IdType="pubmed">15109248</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>EMBO J. 2002 Jul 1;21(13):3213-24</Citation><ArticleIdList><ArticleId IdType="pubmed">12093723</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Med Chem. 2002 Nov 7;45(23):4958-60</Citation><ArticleIdList><ArticleId IdType="pubmed">12408706</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2001 Jul;75(14):6676-81</Citation><ArticleIdList><ArticleId IdType="pubmed">11413334</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Med Chem. 2004 Dec 2;47(25):6113-6</Citation><ArticleIdList><ArticleId IdType="pubmed">15566280</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Med Chem. 2004 Mar 11;47(6):1553-74</Citation><ArticleIdList><ArticleId IdType="pubmed">14998341</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Mol Biol. 1986 Aug 20;190(4):593-604</Citation><ArticleIdList><ArticleId IdType="pubmed">3097327</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2004 Apr 20;43(15):4568-74</Citation><ArticleIdList><ArticleId IdType="pubmed">15078103</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Chem Biol. 2004 Sep;11(9):1293-9</Citation><ArticleIdList><ArticleId IdType="pubmed">15380189</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Eur J Med Chem. 2005 Jan;40(1):57-62</Citation><ArticleIdList><ArticleId IdType="pubmed">15642409</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):760-3</Citation><ArticleIdList><ArticleId IdType="pubmed">15299374</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Struct Biol. 1999 Apr-May;125(2-3):156-65</Citation><ArticleIdList><ArticleId IdType="pubmed">10222271</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2005 Jan 7;280(1):164-73</Citation><ArticleIdList><ArticleId IdType="pubmed">15507456</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>N Engl J Med. 2003 May 15;348(20):1953-66</Citation><ArticleIdList><ArticleId IdType="pubmed">12690092</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):240-55</Citation><ArticleIdList><ArticleId IdType="pubmed">15299926</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Chem Biol. 2004 Oct;11(10):1445-53</Citation><ArticleIdList><ArticleId IdType="pubmed">15489171</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Jul 6;101(27):10012-7</Citation><ArticleIdList><ArticleId IdType="pubmed">15226499</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>N Engl J Med. 2003 May 15;348(20):1967-76</Citation><ArticleIdList><ArticleId IdType="pubmed">12690091</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Gen Virol. 2000 Apr;81(Pt 4):853-79</Citation><ArticleIdList><ArticleId IdType="pubmed">10725411</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 1989 Feb 7;28(3):1330-2</Citation><ArticleIdList><ArticleId IdType="pubmed">2713367</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biol Chem. 2003 Dec;384(12):1613-8</Citation><ArticleIdList><ArticleId IdType="pubmed">14719804</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2004 Nov 30;43(47):14958-70</Citation><ArticleIdList><ArticleId IdType="pubmed">15554703</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Science. 2003 Jun 13;300(5626):1763-7</Citation><ArticleIdList><ArticleId IdType="pubmed">12746549</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1131-7</Citation><ArticleIdList><ArticleId IdType="pubmed">12832755</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Chem Inf Model. 2005 Jan-Feb;45(1):10-17</Citation><ArticleIdList><ArticleId IdType="pubmed">15667124</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Gen Virol. 2003 Sep;84(Pt 9):2305-2315</Citation><ArticleIdList><ArticleId IdType="pubmed">12917450</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2003 Nov 11;100(23):13190-5</Citation><ArticleIdList><ArticleId IdType="pubmed">14585926</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Chem Rev. 2002 Dec;102(12):4639-750</Citation><ArticleIdList><ArticleId IdType="pubmed">12475205</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Respir Res. 2005 Jan 20;6:8</Citation><ArticleIdList><ArticleId IdType="pubmed">15661082</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Protein Eng. 1995 Feb;8(2):127-34</Citation><ArticleIdList><ArticleId IdType="pubmed">7630882</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Cell Death Differ. 2003 Aug;10(8):881-8</Citation><ArticleIdList><ArticleId IdType="pubmed">12867995</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 1967 Apr 20;27(2):157-62</Citation><ArticleIdList><ArticleId IdType="pubmed">6035483</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Lancet. 2003 Apr 19;361(9366):1319-25</Citation><ArticleIdList><ArticleId IdType="pubmed">12711465</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country></list><tree><noCountry><name sortKey="Cherney, Maia M" sort="Cherney, Maia M" uniqKey="Cherney M" first="Maia M" last="Cherney">Maia M. Cherney</name><name sortKey="Eltis, Lindsay D" sort="Eltis, Lindsay D" uniqKey="Eltis L" first="Lindsay D" last="Eltis">Lindsay D. Eltis</name><name sortKey="Huitema, Carly" sort="Huitema, Carly" uniqKey="Huitema C" first="Carly" last="Huitema">Carly Huitema</name><name sortKey="James, Karen Ellis" sort="James, Karen Ellis" uniqKey="James K" first="Karen Ellis" last="James">Karen Ellis James</name><name sortKey="James, Michael N G" sort="James, Michael N G" uniqKey="James M" first="Michael N G" last="James">Michael N G. James</name><name sortKey="Liu, Jie" sort="Liu, Jie" uniqKey="Liu J" first="Jie" last="Liu">Jie Liu</name><name sortKey="Powers, James C" sort="Powers, James C" uniqKey="Powers J" first="James C" last="Powers">James C. Powers</name></noCountry><country name="Canada"><noRegion><name sortKey="Lee, Ting Wai" sort="Lee, Ting Wai" uniqKey="Lee T" first="Ting-Wai" last="Lee">Ting-Wai Lee</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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