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Mutation of Gly-11 on the dimer interface results in the complete crystallographic dimer dissociation of severe acute respiratory syndrome coronavirus 3C-like protease: crystal structure with molecular dynamics simulations.

Identifieur interne : 001B01 ( Ncbi/Merge ); précédent : 001B00; suivant : 001B02

Mutation of Gly-11 on the dimer interface results in the complete crystallographic dimer dissociation of severe acute respiratory syndrome coronavirus 3C-like protease: crystal structure with molecular dynamics simulations.

Auteurs : Shuai Chen ; Tiancen Hu ; Jian Zhang ; Jing Chen ; Kaixian Chen ; Jianping Ding ; Hualiang Jiang ; Xu Shen

Source :

The Journal of biological chemistry [ 0021-9258 ] ; 2008.

RBID : pubmed:17977841

Descripteurs français

English descriptors

KwdEn :
- Circular Dichroism, Computer Simulation, Crystallography, X-Ray, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (genetics), Cysteine Endopeptidases (metabolism), Dimerization, Glycine (genetics), Models, Molecular, Mutation, Promoter Regions, Genetic (genetics), Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary, SARS Virus (enzymology), Spectrometry, Fluorescence, Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (metabolism).
MESH :
- chemical , chemistry : Cysteine Endopeptidases, Viral Proteins.
- chemical , genetics : Cysteine Endopeptidases, Glycine, Viral Proteins.
- chemical , metabolism : Cysteine Endopeptidases, Viral Proteins.
- enzymology : SARS Virus.
- genetics : Promoter Regions, Genetic.
- Circular Dichroism, Computer Simulation, Crystallography, X-Ray, Dimerization, Models, Molecular, Mutation, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary, Spectrometry, Fluorescence.

Abstract

SARS-CoV 3C-like protease (3CL(pro)) is an attractive target for anti-severe acute respiratory syndrome (SARS) drug discovery, and its dimerization has been extensively proved to be indispensable for enzymatic activity. However, the reason why the dissociated monomer is inactive still remains unclear due to the absence of the monomer structure. In this study, we showed that mutation of the dimer-interface residue Gly-11 to alanine entirely abolished the activity of SARS-CoV 3CL(pro). Subsequently, we determined the crystal structure of this mutant and discovered a complete crystallographic dimer dissociation of SARS-CoV 3CL(pro). The mutation might shorten the alpha-helix A' of domain I and cause a mis-oriented N-terminal finger that could not correctly squeeze into the pocket of another monomer during dimerization, thus destabilizing the dimer structure. Several structural features essential for catalysis and substrate recognition are severely impaired in the G11A monomer. Moreover, domain III rotates dramatically against the chymotrypsin fold compared with the dimer, from which we proposed a putative dimerization model for SARS-CoV 3CL(pro). As the first reported monomer structure for SARS-CoV 3CL(pro), the crystal structure of G11A mutant might provide insight into the dimerization mechanism of the protease and supply direct structural evidence for the incompetence of the dissociated monomer.

DOI: 10.1074/jbc.M705240200
PubMed: 17977841

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<author><name sortKey="Chen, Kaixian" sort="Chen, Kaixian" uniqKey="Chen K" first="Kaixian" last="Chen">Kaixian Chen</name>
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<author><name sortKey="Chen, Jing" sort="Chen, Jing" uniqKey="Chen J" first="Jing" last="Chen">Jing Chen</name>
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<term>Computer Simulation</term>
<term>Crystallography, X-Ray</term>
<term>Cysteine Endopeptidases (chemistry)</term>
<term>Cysteine Endopeptidases (genetics)</term>
<term>Cysteine Endopeptidases (metabolism)</term>
<term>Dimerization</term>
<term>Glycine (genetics)</term>
<term>Models, Molecular</term>
<term>Mutation</term>
<term>Promoter Regions, Genetic (genetics)</term>
<term>Protein Binding</term>
<term>Protein Structure, Secondary</term>
<term>Protein Structure, Tertiary</term>
<term>SARS Virus (enzymology)</term>
<term>Spectrometry, Fluorescence</term>
<term>Viral Proteins (chemistry)</term>
<term>Viral Proteins (genetics)</term>
<term>Viral Proteins (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Cristallographie aux rayons X</term>
<term>Cysteine endopeptidases ()</term>
<term>Cysteine endopeptidases (génétique)</term>
<term>Cysteine endopeptidases (métabolisme)</term>
<term>Dichroïsme circulaire</term>
<term>Dimérisation</term>
<term>Glycine (génétique)</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Mutation</term>
<term>Protéines virales ()</term>
<term>Protéines virales (génétique)</term>
<term>Protéines virales (métabolisme)</term>
<term>Régions promotrices (génétique) (génétique)</term>
<term>Simulation numérique</term>
<term>Spectrométrie de fluorescence</term>
<term>Structure secondaire des protéines</term>
<term>Structure tertiaire des protéines</term>
<term>Virus du SRAS (enzymologie)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine Endopeptidases</term>
<term>Viral Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cysteine Endopeptidases</term>
<term>Glycine</term>
<term>Viral Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine Endopeptidases</term>
<term>Viral Proteins</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Promoter Regions, Genetic</term>
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<term>Glycine</term>
<term>Protéines virales</term>
<term>Régions promotrices (génétique)</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cysteine endopeptidases</term>
<term>Protéines virales</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Circular Dichroism</term>
<term>Computer Simulation</term>
<term>Crystallography, X-Ray</term>
<term>Dimerization</term>
<term>Models, Molecular</term>
<term>Mutation</term>
<term>Protein Binding</term>
<term>Protein Structure, Secondary</term>
<term>Protein Structure, Tertiary</term>
<term>Spectrometry, Fluorescence</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Cristallographie aux rayons X</term>
<term>Cysteine endopeptidases</term>
<term>Dichroïsme circulaire</term>
<term>Dimérisation</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Mutation</term>
<term>Protéines virales</term>
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<front><div type="abstract" xml:lang="en">SARS-CoV 3C-like protease (3CL(pro)) is an attractive target for anti-severe acute respiratory syndrome (SARS) drug discovery, and its dimerization has been extensively proved to be indispensable for enzymatic activity. However, the reason why the dissociated monomer is inactive still remains unclear due to the absence of the monomer structure. In this study, we showed that mutation of the dimer-interface residue Gly-11 to alanine entirely abolished the activity of SARS-CoV 3CL(pro). Subsequently, we determined the crystal structure of this mutant and discovered a complete crystallographic dimer dissociation of SARS-CoV 3CL(pro). The mutation might shorten the alpha-helix A' of domain I and cause a mis-oriented N-terminal finger that could not correctly squeeze into the pocket of another monomer during dimerization, thus destabilizing the dimer structure. Several structural features essential for catalysis and substrate recognition are severely impaired in the G11A monomer. Moreover, domain III rotates dramatically against the chymotrypsin fold compared with the dimer, from which we proposed a putative dimerization model for SARS-CoV 3CL(pro). As the first reported monomer structure for SARS-CoV 3CL(pro), the crystal structure of G11A mutant might provide insight into the dimerization mechanism of the protease and supply direct structural evidence for the incompetence of the dissociated monomer.</div>
</front>
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<Month>06</Month>
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<ArticleTitle>Mutation of Gly-11 on the dimer interface results in the complete crystallographic dimer dissociation of severe acute respiratory syndrome coronavirus 3C-like protease: crystal structure with molecular dynamics simulations.</ArticleTitle>
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<Abstract><AbstractText>SARS-CoV 3C-like protease (3CL(pro)) is an attractive target for anti-severe acute respiratory syndrome (SARS) drug discovery, and its dimerization has been extensively proved to be indispensable for enzymatic activity. However, the reason why the dissociated monomer is inactive still remains unclear due to the absence of the monomer structure. In this study, we showed that mutation of the dimer-interface residue Gly-11 to alanine entirely abolished the activity of SARS-CoV 3CL(pro). Subsequently, we determined the crystal structure of this mutant and discovered a complete crystallographic dimer dissociation of SARS-CoV 3CL(pro). The mutation might shorten the alpha-helix A' of domain I and cause a mis-oriented N-terminal finger that could not correctly squeeze into the pocket of another monomer during dimerization, thus destabilizing the dimer structure. Several structural features essential for catalysis and substrate recognition are severely impaired in the G11A monomer. Moreover, domain III rotates dramatically against the chymotrypsin fold compared with the dimer, from which we proposed a putative dimerization model for SARS-CoV 3CL(pro). As the first reported monomer structure for SARS-CoV 3CL(pro), the crystal structure of G11A mutant might provide insight into the dimerization mechanism of the protease and supply direct structural evidence for the incompetence of the dissociated monomer.</AbstractText>
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<name sortKey="Chen, Shuai" sort="Chen, Shuai" uniqKey="Chen S" first="Shuai" last="Chen">Shuai Chen</name>
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Mutation of Gly-11 on the dimer interface results in the complete crystallographic dimer dissociation of severe acute respiratory syndrome coronavirus 3C-like protease: crystal structure with molecular dynamics simulations.

Mutation of Gly-11 on the dimer interface results in the complete crystallographic dimer dissociation of severe acute respiratory syndrome coronavirus 3C-like protease: crystal structure with molecular dynamics simulations.

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