Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra α-helical domain
Identifieur interne : 000020 ( Ncbi/Checkpoint ); précédent : 000019; suivant : 000021Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra α-helical domain
Auteurs : Kanchan Anand ; Gottfried J. Palm ; Jeroen R. Mesters ; Stuart G. Siddell ; John Ziebuhr ; Rolf HilgenfeldSource :
- The EMBO Journal [ 0261-4189 ] ; 2002.
Descripteurs français
- KwdFr :
- Alignement de séquences, Chymotrypsine (), Conformation des protéines, Cristallographie aux rayons X, Cysteine endopeptidases (), Cysteine endopeptidases (génétique), Dimérisation, Données de séquences moléculaires, Liaison aux protéines, Modèles moléculaires, Mutagenèse, Pliage des protéines, Protéines de fusion recombinantes (), Similitude de séquences d'acides aminés, Sites de fixation, Structure tertiaire des protéines, Séquence d'acides aminés, Virus de la gastroentérite transmissible (enzymologie), Virus de la gastroentérite transmissible (génétique).
- MESH :
- enzymologie : Virus de la gastroentérite transmissible.
- génétique : Cysteine endopeptidases, Virus de la gastroentérite transmissible.
- Alignement de séquences, Chymotrypsine, Conformation des protéines, Cristallographie aux rayons X, Cysteine endopeptidases, Dimérisation, Données de séquences moléculaires, Liaison aux protéines, Modèles moléculaires, Mutagenèse, Pliage des protéines, Protéines de fusion recombinantes, Similitude de séquences d'acides aminés, Sites de fixation, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Binding Sites, Chymotrypsin (chemistry), Crystallography, X-Ray, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (genetics), Dimerization, Models, Molecular, Molecular Sequence Data, Mutagenesis, Protein Binding, Protein Conformation, Protein Folding, Protein Structure, Tertiary, Recombinant Fusion Proteins (chemistry), Sequence Alignment, Sequence Homology, Amino Acid, Transmissible gastroenteritis virus (enzymology), Transmissible gastroenteritis virus (genetics).
- MESH :
- chemical , chemistry : Chymotrypsin, Cysteine Endopeptidases, Recombinant Fusion Proteins.
- chemical , genetics : Cysteine Endopeptidases.
- enzymology : Transmissible gastroenteritis virus.
- genetics : Transmissible gastroenteritis virus.
- Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, Dimerization, Models, Molecular, Molecular Sequence Data, Mutagenesis, Protein Binding, Protein Conformation, Protein Folding, Protein Structure, Tertiary, Sequence Alignment, Sequence Homology, Amino Acid.
Abstract
The key enzyme in coronavirus polyprotein processing is the viral main proteinase, Mpro, a protein with extremely low sequence similarity to other viral and cellular proteinases. Here, the crystal structure of the 33.1 kDa transmissible gastroenteritis (corona)virus Mpro is reported. The structure was refined to 1.96 Å resolution and revealed three dimers in the asymmetric unit. The mutual arrangement of the protomers in each of the dimers suggests that Mpro self-processing occurs
Url:
DOI: 10.1093/emboj/cdf327
PubMed: 12093723
PubMed Central: 126080
Affiliations:
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PMC:126080Le document en format XML
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Siddell</name><affiliation><nlm:aff id="N0x99a9038.0x98cb100"></nlm:aff></affiliation></author><author><name sortKey="Ziebuhr, John" sort="Ziebuhr, John" uniqKey="Ziebuhr J" first="John" last="Ziebuhr">John Ziebuhr</name><affiliation><nlm:aff id="N0x99a9038.0x98cb100"></nlm:aff></affiliation><affiliation><nlm:aff id="N0x99a9038.0x98cb100"></nlm:aff></affiliation></author><author><name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name><affiliation><nlm:aff id="N0x99a9038.0x98cb100"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">12093723</idno><idno type="pmc">126080</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC126080</idno><idno type="RBID">PMC:126080</idno><idno type="doi">10.1093/emboj/cdf327</idno><date when="2002">2002</date><idno type="wicri:Area/Pmc/Corpus">000449</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000449</idno><idno type="wicri:Area/Pmc/Curation">000449</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000449</idno><idno type="wicri:Area/Pmc/Checkpoint">000A14</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000A14</idno><idno type="wicri:source">PubMed</idno><idno type="RBID">pubmed:12093723</idno><idno type="wicri:Area/PubMed/Corpus">000D75</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000D75</idno><idno type="wicri:Area/PubMed/Curation">000D75</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000D75</idno><idno type="wicri:Area/PubMed/Checkpoint">000D56</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000D56</idno><idno type="wicri:Area/Ncbi/Merge">000020</idno><idno type="wicri:Area/Ncbi/Curation">000020</idno><idno type="wicri:Area/Ncbi/Checkpoint">000020</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra α-helical domain</title><author><name sortKey="Anand, Kanchan" sort="Anand, Kanchan" uniqKey="Anand K" first="Kanchan" last="Anand">Kanchan Anand</name></author><author><name sortKey="Palm, Gottfried J" sort="Palm, Gottfried J" uniqKey="Palm G" first="Gottfried J." last="Palm">Gottfried J. Palm</name></author><author><name sortKey="Mesters, Jeroen R" sort="Mesters, Jeroen R" uniqKey="Mesters J" first="Jeroen R." last="Mesters">Jeroen R. Mesters</name></author><author><name sortKey="Siddell, Stuart G" sort="Siddell, Stuart G" uniqKey="Siddell S" first="Stuart G." last="Siddell">Stuart G. Siddell</name><affiliation><nlm:aff id="N0x99a9038.0x98cb100"></nlm:aff></affiliation></author><author><name sortKey="Ziebuhr, John" sort="Ziebuhr, John" uniqKey="Ziebuhr J" first="John" last="Ziebuhr">John Ziebuhr</name><affiliation><nlm:aff id="N0x99a9038.0x98cb100"></nlm:aff></affiliation><affiliation><nlm:aff id="N0x99a9038.0x98cb100"></nlm:aff></affiliation></author><author><name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name><affiliation><nlm:aff id="N0x99a9038.0x98cb100"></nlm:aff></affiliation></author></analytic><series><title level="j">The EMBO Journal</title><idno type="ISSN">0261-4189</idno><idno type="eISSN">1460-2075</idno><imprint><date when="2002">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Chymotrypsin (chemistry)</term><term>Crystallography, X-Ray</term><term>Cysteine Endopeptidases (chemistry)</term><term>Cysteine Endopeptidases (genetics)</term><term>Dimerization</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Mutagenesis</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Folding</term><term>Protein Structure, Tertiary</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term><term>Transmissible gastroenteritis virus (enzymology)</term><term>Transmissible gastroenteritis virus (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences</term><term>Chymotrypsine ()</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Cysteine endopeptidases ()</term><term>Cysteine endopeptidases (génétique)</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Mutagenèse</term><term>Pliage des protéines</term><term>Protéines de fusion recombinantes ()</term><term>Similitude de séquences d'acides aminés</term><term>Sites de fixation</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Virus de la gastroentérite transmissible (enzymologie)</term><term>Virus de la gastroentérite transmissible (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Chymotrypsin</term><term>Cysteine Endopeptidases</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cysteine Endopeptidases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus de la gastroentérite transmissible</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Transmissible gastroenteritis virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Transmissible gastroenteritis virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cysteine endopeptidases</term><term>Virus de la gastroentérite transmissible</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Crystallography, X-Ray</term><term>Dimerization</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Mutagenesis</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Folding</term><term>Protein Structure, Tertiary</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Chymotrypsine</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Cysteine endopeptidases</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Mutagenèse</term><term>Pliage des protéines</term><term>Protéines de fusion recombinantes</term><term>Similitude de séquences d'acides aminés</term><term>Sites de fixation</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The key enzyme in coronavirus polyprotein processing is the viral main proteinase, M<sup>pro</sup>, a protein with extremely low sequence similarity to other viral and cellular proteinases. Here, the crystal structure of the 33.1 kDa transmissible gastroenteritis (corona)virus M<sup>pro</sup> is reported. The structure was refined to 1.96 Å resolution and revealed three dimers in the asymmetric unit. The mutual arrangement of the protomers in each of the dimers suggests that M<sup>pro</sup> self-processing occurs <italic>in trans</italic>. The active site, comprised of Cys144 and His41, is part of a chymotrypsin-like fold that is connected by a 16 residue loop to an extra domain featuring a novel α-helical fold. Molecular modelling and mutagenesis data implicate the loop in substrate binding and elucidate S1 and S2 subsites suitable to accommodate the side chains of the P1 glutamine and P2 leucine residues of M<sup>pro</sup> substrates. Interactions involving the N-terminus and the α-helical domain stabilize the loop in the orientation required for <italic>trans</italic>-cleavage activity. The study illustrates that RNA viruses have evolved unprecedented variations of the classical chymotrypsin fold.</p></div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Anand, Kanchan" sort="Anand, Kanchan" uniqKey="Anand K" first="Kanchan" last="Anand">Kanchan Anand</name><name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name><name sortKey="Mesters, Jeroen R" sort="Mesters, Jeroen R" uniqKey="Mesters J" first="Jeroen R." last="Mesters">Jeroen R. Mesters</name><name sortKey="Palm, Gottfried J" sort="Palm, Gottfried J" uniqKey="Palm G" first="Gottfried J." last="Palm">Gottfried J. Palm</name><name sortKey="Siddell, Stuart G" sort="Siddell, Stuart G" uniqKey="Siddell S" first="Stuart G." last="Siddell">Stuart G. Siddell</name><name sortKey="Ziebuhr, John" sort="Ziebuhr, John" uniqKey="Ziebuhr J" first="John" last="Ziebuhr">John Ziebuhr</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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