CovidV1, PubMed, Checkpoint, bibRecord, 000712

Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain.

Identifieur interne : 000712 ( PubMed/Checkpoint ); précédent : 000711; suivant : 000713

Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain.

Auteurs : Kanchan Anand [Allemagne] ; Gottfried J. Palm ; Jeroen R. Mesters ; Stuart G. Siddell ; John Ziebuhr ; Rolf Hilgenfeld

Source :

The EMBO journal [ 0261-4189 ] ; 2002.

RBID : pubmed:12093723

Descripteurs français

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, M(pro), 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(pro) is reported. The structure was refined to 1.96 A resolution and revealed three dimers in the asymmetric unit. The mutual arrangement of the protomers in each of the dimers suggests that M(pro) self-processing occurs in trans. 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 alpha-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(pro) substrates. Interactions involving the N-terminus and the alpha-helical domain stabilize the loop in the orientation required for trans-cleavage activity. The study illustrates that RNA viruses have evolved unprecedented variations of the classical chymotrypsin fold.

DOI: 10.1093/emboj/cdf327
PubMed: 12093723

Affiliations:

Allemagne

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 000721
to stream PubMed, to step Curation: 000721

Links to Exploration step

pubmed:12093723

Le document en format XML

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<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>
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<term>Transmissible gastroenteritis virus (genetics)</term>
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<term>Chymotrypsine ()</term>
<term>Conformation des protéines</term>
<term>Cristallographie aux rayons X</term>
<term>Cysteine endopeptidases ()</term>
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<term>Données de séquences moléculaires</term>
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<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>
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<term>Cysteine Endopeptidases</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cysteine Endopeptidases</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus de la gastroentérite transmissible</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Transmissible gastroenteritis virus</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cysteine endopeptidases</term>
<term>Virus de la gastroentérite transmissible</term>
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<term>Protein Folding</term>
<term>Protein Structure, Tertiary</term>
<term>Sequence Alignment</term>
<term>Sequence Homology, Amino Acid</term>
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<term>Conformation des protéines</term>
<term>Cristallographie aux rayons X</term>
<term>Cysteine endopeptidases</term>
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<front><div type="abstract" xml:lang="en">The key enzyme in coronavirus polyprotein processing is the viral main proteinase, M(pro), 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(pro) is reported. The structure was refined to 1.96 A resolution and revealed three dimers in the asymmetric unit. The mutual arrangement of the protomers in each of the dimers suggests that M(pro) self-processing occurs in trans. 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 alpha-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(pro) substrates. Interactions involving the N-terminus and the alpha-helical domain stabilize the loop in the orientation required for trans-cleavage activity. The study illustrates that RNA viruses have evolved unprecedented variations of the classical chymotrypsin fold.</div>
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<Abstract><AbstractText>The key enzyme in coronavirus polyprotein processing is the viral main proteinase, M(pro), 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(pro) is reported. The structure was refined to 1.96 A resolution and revealed three dimers in the asymmetric unit. The mutual arrangement of the protomers in each of the dimers suggests that M(pro) self-processing occurs in trans. 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 alpha-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(pro) substrates. Interactions involving the N-terminus and the alpha-helical domain stabilize the loop in the orientation required for trans-cleavage activity. The study illustrates that RNA viruses have evolved unprecedented variations of the classical chymotrypsin fold.</AbstractText>
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<ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):191-205</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10089410</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Bioinformatics. 1999 Apr;15(4):317-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10320400</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1999 Sep 28;96(20):11000-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10500114</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1999 Oct 15;18(20):5463-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10523291</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 2000 Apr;81(Pt 4):853-79</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10725411</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 2000 Jun 20;272(1):27-39</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10873746</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virus Genes. 2001;23(1):105-18</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11556396</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 2002 Mar;83(Pt 3):581-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11842253</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 2002 Mar;83(Pt 3):595-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11842254</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PCR Methods Appl. 1992 Feb;1(3):205-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1335326</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):760-3</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15299374</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):43-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15299724</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proteins. 1991;11(4):281-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1758883</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1992 Jan 30;355(6359):472-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18481394</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1991 Jun;65(6):2910-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1851863</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr A. 1991 Mar 1;47 ( Pt 2):110-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2025413</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1990 May;9(5):1665-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2184035</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Microbiol. 1990;44:603-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2252396</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Graph. 1990 Mar;8(1):52-6, 29</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2268628</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 1989 Jun 26;17(12):4847-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2526320</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS Lett. 1989 Jan 30;243(2):103-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2645167</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1997;276:307-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27754618</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1988 Nov;85(21):7872-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3186696</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1987 May 20;195(2):397-418</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3477645</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1985 Aug 5;184(3):479-502</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3900416</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1985 Aug 20;184(4):703-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">4046030</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS Lett. 1974 Oct 1;47(1):15-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">4426388</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1971 Feb 14;55(3):379-400</Citation>
<ArticleIdList><ArticleId IdType="pubmed">5551392</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1968 Apr 28;33(2):491-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">5700707</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1984 Oct 25;179(2):233-56</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6502713</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1980 Nov 25;144(1):43-88</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6783761</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1994 Jun 3;77(5):761-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7515772</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1995 Jun;69(6):3554-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7745703</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1995 Jun;69(6):3658-67</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7745714</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1995 Jul;69(7):4331-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7769694</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1995 Jun 1;209(2):420-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7778277</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1995 Feb 1;206(2):817-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7856095</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1994 May 5;369(6475):72-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8164744</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1993 Dec 5;268(34):25735-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8245010</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1993 Sep;12(9):3587-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8253083</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1993 Sep 5;233(1):123-38</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8377180</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Protein Sci. 1995 Aug;4(8):1439-45</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8520469</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1996 Aug 15;222(2):375-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8806521</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1997 Jan;78 ( Pt 1):71-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9010287</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1997 Mar;71(3):2436-48</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9032381</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1997 May;71(5):3992-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9094676</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1997 Apr 14;230(2):335-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9143289</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Arch Virol. 1997;142(3):629-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9349308</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1997 Nov 14;273(5):1032-47</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9367789</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 1997 Dec 15;25(24):4876-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9396791</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1998 Mar 15;242(2):288-302</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9514967</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):905-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9757107</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1999 Jan;73(1):177-85</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9847320</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain.

Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain.

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