Critical assessment of important regions in the subunit association and catalytic action of the severe acute respiratory syndrome coronavirus main protease.
Identifieur interne : 004878 ( Main/Exploration ); précédent : 004877; suivant : 004879Critical assessment of important regions in the subunit association and catalytic action of the severe acute respiratory syndrome coronavirus main protease.
Auteurs : Wen-Chi Hsu [Taïwan] ; Hui-Chuan Chang ; Chi-Yuan Chou ; Pui-Jen Tsai ; Pei-In Lin ; Gu-Gang ChangSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2005.
Descripteurs français
- KwdFr :
- ARN viral (), Catalyse, Chymotrypsine (), Cinétique, Cristallographie aux rayons X, Cysteine endopeptidases, Dichroïsme circulaire, Dimérisation, Délétion de gène, Endopeptidases (), Endopeptidases (métabolisme), Escherichia coli (métabolisme), Modèles moléculaires, Modèles statistiques, Pliage des protéines, Protéines virales (), Protéines virales (métabolisme), Spectrométrie de fluorescence, Structure quaternaire des protéines, Structure tertiaire des protéines, Ultracentrifugation, Virus du SRAS (enzymologie).
- MESH :
- enzymologie : Virus du SRAS.
- métabolisme : Endopeptidases, Escherichia coli, Protéines virales.
- ARN viral, Catalyse, Chymotrypsine, Cinétique, Cristallographie aux rayons X, Cysteine endopeptidases, Dichroïsme circulaire, Dimérisation, Délétion de gène, Endopeptidases, Modèles moléculaires, Modèles statistiques, Pliage des protéines, Protéines virales, Spectrométrie de fluorescence, Structure quaternaire des protéines, Structure tertiaire des protéines, Ultracentrifugation.
English descriptors
- KwdEn :
- Catalysis, Chymotrypsin (chemistry), Circular Dichroism, Crystallography, X-Ray, Cysteine Endopeptidases, Dimerization, Endopeptidases (chemistry), Endopeptidases (metabolism), Escherichia coli (metabolism), Gene Deletion, Kinetics, Models, Molecular, Models, Statistical, Protein Folding, Protein Structure, Quaternary, Protein Structure, Tertiary, RNA, Viral (chemistry), SARS Virus (enzymology), Spectrometry, Fluorescence, Ultracentrifugation, Viral Proteins (chemistry), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Chymotrypsin, Endopeptidases, RNA, Viral, Viral Proteins.
- chemical , metabolism : Endopeptidases, Viral Proteins.
- enzymology : SARS Virus.
- metabolism : Escherichia coli.
- Catalysis, Circular Dichroism, Crystallography, X-Ray, Cysteine Endopeptidases, Dimerization, Gene Deletion, Kinetics, Models, Molecular, Models, Statistical, Protein Folding, Protein Structure, Quaternary, Protein Structure, Tertiary, Spectrometry, Fluorescence, Ultracentrifugation.
Abstract
The severe acute respiratory syndrome (SARS) coronavirus (CoV) main protease represents an attractive target for the development of novel anti-SARS agents. The tertiary structure of the protease consists of two distinct folds. One is the N-terminal chymotrypsin-like fold that consists of two structural domains and constitutes the catalytic machinery; the other is the C-terminal helical domain, which has an unclear function and is not found in other RNA virus main proteases. To understand the functional roles of the two structural parts of the SARS-CoV main protease, we generated the full-length of this enzyme as well as several terminally truncated forms, different from each other only by the number of amino acid residues at the C- or N-terminal regions. The quaternary structure and K(d) value of the protease were analyzed by analytical ultracentrifugation. The results showed that the N-terminal 1-3 amino acid-truncated protease maintains 76% of enzyme activity and that the major form is a dimer, as in the wild type. However, the amino acids 1-4-truncated protease showed the major form to be a monomer and had little enzyme activity. As a result, the fourth amino acid seemed to have a powerful effect on the quaternary structure and activity of this protease. The last C-terminal helically truncated protease also exhibited a greater tendency to form monomer and showed little activity. We concluded that both the C- and the N-terminal regions influence the dimerization and enzyme activity of the SARS-CoV main protease.
DOI: 10.1074/jbc.M502556200
PubMed: 15831489
Affiliations:
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sort="Chou, Chi Yuan" uniqKey="Chou C" first="Chi-Yuan" last="Chou">Chi-Yuan Chou</name></author><author><name sortKey="Tsai, Pui Jen" sort="Tsai, Pui Jen" uniqKey="Tsai P" first="Pui-Jen" last="Tsai">Pui-Jen Tsai</name></author><author><name sortKey="Lin, Pei In" sort="Lin, Pei In" uniqKey="Lin P" first="Pei-In" last="Lin">Pei-In Lin</name></author><author><name sortKey="Chang, Gu Gang" sort="Chang, Gu Gang" uniqKey="Chang G" first="Gu-Gang" last="Chang">Gu-Gang Chang</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:15831489</idno><idno type="pmid">15831489</idno><idno type="doi">10.1074/jbc.M502556200</idno><idno type="wicri:Area/PubMed/Corpus">002791</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002791</idno><idno type="wicri:Area/PubMed/Curation">002791</idno><idno type="wicri:explorRef" wicri:stream="PubMed" 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of Biochemistry, and Structural Biology Program, National Yang-Ming University, Taipei 112, Taiwan.</nlm:affiliation><country xml:lang="fr">Taïwan</country><wicri:regionArea>Faculty of Life Sciences, Institute of Biochemistry, and Structural Biology Program, National Yang-Ming University, Taipei 112</wicri:regionArea><wicri:noRegion>Taipei 112</wicri:noRegion></affiliation></author><author><name sortKey="Chang, Hui Chuan" sort="Chang, Hui Chuan" uniqKey="Chang H" first="Hui-Chuan" last="Chang">Hui-Chuan Chang</name></author><author><name sortKey="Chou, Chi Yuan" sort="Chou, Chi Yuan" uniqKey="Chou C" first="Chi-Yuan" last="Chou">Chi-Yuan Chou</name></author><author><name sortKey="Tsai, Pui Jen" sort="Tsai, Pui Jen" uniqKey="Tsai P" first="Pui-Jen" last="Tsai">Pui-Jen Tsai</name></author><author><name sortKey="Lin, Pei In" sort="Lin, Pei In" uniqKey="Lin P" first="Pei-In" last="Lin">Pei-In Lin</name></author><author><name sortKey="Chang, Gu Gang" sort="Chang, Gu Gang" uniqKey="Chang G" first="Gu-Gang" last="Chang">Gu-Gang Chang</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Catalysis</term><term>Chymotrypsin (chemistry)</term><term>Circular Dichroism</term><term>Crystallography, X-Ray</term><term>Cysteine Endopeptidases</term><term>Dimerization</term><term>Endopeptidases (chemistry)</term><term>Endopeptidases (metabolism)</term><term>Escherichia coli (metabolism)</term><term>Gene Deletion</term><term>Kinetics</term><term>Models, Molecular</term><term>Models, Statistical</term><term>Protein Folding</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Tertiary</term><term>RNA, Viral (chemistry)</term><term>SARS Virus (enzymology)</term><term>Spectrometry, Fluorescence</term><term>Ultracentrifugation</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN viral ()</term><term>Catalyse</term><term>Chymotrypsine ()</term><term>Cinétique</term><term>Cristallographie aux rayons X</term><term>Cysteine endopeptidases</term><term>Dichroïsme circulaire</term><term>Dimérisation</term><term>Délétion de gène</term><term>Endopeptidases ()</term><term>Endopeptidases (métabolisme)</term><term>Escherichia coli (métabolisme)</term><term>Modèles moléculaires</term><term>Modèles statistiques</term><term>Pliage des protéines</term><term>Protéines virales ()</term><term>Protéines virales (métabolisme)</term><term>Spectrométrie de fluorescence</term><term>Structure quaternaire des protéines</term><term>Structure tertiaire des protéines</term><term>Ultracentrifugation</term><term>Virus du SRAS (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Chymotrypsin</term><term>Endopeptidases</term><term>RNA, Viral</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Endopeptidases</term><term>Viral Proteins</term></keywords><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></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Endopeptidases</term><term>Escherichia coli</term><term>Protéines virales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalysis</term><term>Circular Dichroism</term><term>Crystallography, X-Ray</term><term>Cysteine Endopeptidases</term><term>Dimerization</term><term>Gene Deletion</term><term>Kinetics</term><term>Models, Molecular</term><term>Models, Statistical</term><term>Protein Folding</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Tertiary</term><term>Spectrometry, Fluorescence</term><term>Ultracentrifugation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ARN viral</term><term>Catalyse</term><term>Chymotrypsine</term><term>Cinétique</term><term>Cristallographie aux rayons X</term><term>Cysteine endopeptidases</term><term>Dichroïsme circulaire</term><term>Dimérisation</term><term>Délétion de gène</term><term>Endopeptidases</term><term>Modèles moléculaires</term><term>Modèles statistiques</term><term>Pliage des protéines</term><term>Protéines virales</term><term>Spectrométrie de fluorescence</term><term>Structure quaternaire des protéines</term><term>Structure tertiaire des protéines</term><term>Ultracentrifugation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome (SARS) coronavirus (CoV) main protease represents an attractive target for the development of novel anti-SARS agents. The tertiary structure of the protease consists of two distinct folds. One is the N-terminal chymotrypsin-like fold that consists of two structural domains and constitutes the catalytic machinery; the other is the C-terminal helical domain, which has an unclear function and is not found in other RNA virus main proteases. To understand the functional roles of the two structural parts of the SARS-CoV main protease, we generated the full-length of this enzyme as well as several terminally truncated forms, different from each other only by the number of amino acid residues at the C- or N-terminal regions. The quaternary structure and K(d) value of the protease were analyzed by analytical ultracentrifugation. The results showed that the N-terminal 1-3 amino acid-truncated protease maintains 76% of enzyme activity and that the major form is a dimer, as in the wild type. However, the amino acids 1-4-truncated protease showed the major form to be a monomer and had little enzyme activity. As a result, the fourth amino acid seemed to have a powerful effect on the quaternary structure and activity of this protease. The last C-terminal helically truncated protease also exhibited a greater tendency to form monomer and showed little activity. We concluded that both the C- and the N-terminal regions influence the dimerization and enzyme activity of the SARS-CoV main protease.</div></front></TEI><affiliations><list><country><li>Taïwan</li></country></list><tree><noCountry><name sortKey="Chang, Gu Gang" sort="Chang, Gu Gang" uniqKey="Chang G" first="Gu-Gang" last="Chang">Gu-Gang Chang</name><name sortKey="Chang, Hui Chuan" sort="Chang, Hui Chuan" uniqKey="Chang H" first="Hui-Chuan" last="Chang">Hui-Chuan Chang</name><name sortKey="Chou, Chi Yuan" sort="Chou, Chi Yuan" uniqKey="Chou C" first="Chi-Yuan" last="Chou">Chi-Yuan Chou</name><name sortKey="Lin, Pei In" sort="Lin, Pei In" uniqKey="Lin P" first="Pei-In" last="Lin">Pei-In Lin</name><name sortKey="Tsai, Pui Jen" sort="Tsai, Pui Jen" uniqKey="Tsai P" first="Pui-Jen" last="Tsai">Pui-Jen Tsai</name></noCountry><country name="Taïwan"><noRegion><name sortKey="Hsu, Wen Chi" sort="Hsu, Wen Chi" uniqKey="Hsu W" first="Wen-Chi" last="Hsu">Wen-Chi Hsu</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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