Quaternary structure of the severe acute respiratory syndrome (SARS) coronavirus main protease.
Identifieur interne : 000C21 ( Ncbi/Merge ); précédent : 000C20; suivant : 000C22Quaternary structure of the severe acute respiratory syndrome (SARS) coronavirus main protease.
Auteurs : Chi-Yuan Chou [Taïwan] ; Hui-Chuan Chang ; Wen-Chi Hsu ; Tien-Zheng Lin ; Chao-Hsiung Lin ; Gu-Gang ChangSource :
- Biochemistry [ 0006-2960 ] ; 2004.
Descripteurs français
- KwdFr :
- Biophysique, Chromatographie en phase liquide à haute performance, Chromatographie sur gel, Cinétique, Concentration en ions d'hydrogène, Concentration osmolaire, Cristallographie aux rayons X, Dichroïsme circulaire, Dimérisation, Endopeptidases (), Endopeptidases (génétique), Endopeptidases (isolement et purification), Endopeptidases (métabolisme), Escherichia coli (génétique), Interactions hydrophobes et hydrophiles, Liaison hydrogène, Modèles moléculaires, Mutagenèse dirigée, Peptides (métabolisme), Phénomènes biophysiques, Plasmides, Protéines recombinantes (isolement et purification), Protéines recombinantes (métabolisme), Spectrométrie de fluorescence, Structure quaternaire des protéines, Structure tertiaire des protéines, Substances tampon, Virus du SRAS (enzymologie), Électricité statique.
- MESH :
- enzymologie : Virus du SRAS.
- génétique : Endopeptidases, Escherichia coli.
- isolement et purification : Endopeptidases, Protéines recombinantes.
- métabolisme : Endopeptidases, Peptides, Protéines recombinantes.
- Biophysique, Chromatographie en phase liquide à haute performance, Chromatographie sur gel, Cinétique, Concentration en ions d'hydrogène, Concentration osmolaire, Cristallographie aux rayons X, Dichroïsme circulaire, Dimérisation, Endopeptidases, Interactions hydrophobes et hydrophiles, Liaison hydrogène, Modèles moléculaires, Mutagenèse dirigée, Phénomènes biophysiques, Plasmides, Spectrométrie de fluorescence, Structure quaternaire des protéines, Structure tertiaire des protéines, Substances tampon, Électricité statique.
English descriptors
- KwdEn :
- Biophysical Phenomena, Biophysics, Buffers, Chromatography, Gel, Chromatography, High Pressure Liquid, Circular Dichroism, Crystallography, X-Ray, Dimerization, Endopeptidases (chemistry), Endopeptidases (genetics), Endopeptidases (isolation & purification), Endopeptidases (metabolism), Escherichia coli (genetics), Hydrogen Bonding, Hydrogen-Ion Concentration, Hydrophobic and Hydrophilic Interactions, Kinetics, Models, Molecular, Mutagenesis, Site-Directed, Osmolar Concentration, Peptides (metabolism), Plasmids, Protein Structure, Quaternary, Protein Structure, Tertiary, Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), SARS Virus (enzymology), Spectrometry, Fluorescence, Static Electricity.
- MESH :
- chemical , chemistry : Endopeptidases.
- chemical , genetics : Endopeptidases.
- chemical , isolation & purification : Endopeptidases, Recombinant Proteins.
- chemical , metabolism : Endopeptidases, Peptides, Recombinant Proteins.
- chemical : Buffers.
- enzymology : SARS Virus.
- genetics : Escherichia coli.
- Biophysical Phenomena, Biophysics, Chromatography, Gel, Chromatography, High Pressure Liquid, Circular Dichroism, Crystallography, X-Ray, Dimerization, Hydrogen Bonding, Hydrogen-Ion Concentration, Hydrophobic and Hydrophilic Interactions, Kinetics, Models, Molecular, Mutagenesis, Site-Directed, Osmolar Concentration, Plasmids, Protein Structure, Quaternary, Protein Structure, Tertiary, Spectrometry, Fluorescence, Static Electricity.
Abstract
SARS (severe acute respiratory syndrome) has been one of the most severe viral infectious diseases last year and still remains as a highly risky public health problem around the world. Exploring the types of interactions responsible for structural stabilities of its component protein molecules constitutes one of the approaches to find a destabilization method for the virion particle. In this study, we performed a series of experiments to characterize the quaternary structure of the dimeric coronavirus main protease (M(pro), 3CL(pro)). By using the analytical ultracentrifuge, we demonstrated that the dimeric SARS coronavirus main protease exists as the major form in solution at protein concentration as low as 0.10 mg/mL at neutral pH. The enzyme started to dissociate at acidic and alkali pH values. Ionic strength has profound effect on the dimer stability indicating that the major force involved in the subunit association is ionic interactions. The effect of ionic strength on the protease molecule was reflected by the drastic change of electrostatic potential contour of the enzyme in the presence of NaCl. Analysis of the crystal structures indicated that the interfacial ionic interaction was attributed to the Arg-4...Glu-290 ion pair between the subunits. Detailed examination of the dimer-monomer equilibrium at different pH values reveals apparent pK(a) values of 8.0 +/- 0.2 and 5.0 +/- 0.1 for the Arg-4 and Glu-290, respectively. Mutation at these two positions reduces the association affinity between subunits, and the Glu-290 mutants had diminished enzyme activity. This information is useful in searching for substances that can intervene in the subunit association, which is attractive as a target to neutralize the virulence of SARS coronavirus.
DOI: 10.1021/bi0490237
PubMed: 15554703
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pubmed:15554703Le document en format XML
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en ions d'hydrogène</term><term>Concentration osmolaire</term><term>Cristallographie aux rayons X</term><term>Dichroïsme circulaire</term><term>Dimérisation</term><term>Endopeptidases ()</term><term>Endopeptidases (génétique)</term><term>Endopeptidases (isolement et purification)</term><term>Endopeptidases (métabolisme)</term><term>Escherichia coli (génétique)</term><term>Interactions hydrophobes et hydrophiles</term><term>Liaison hydrogène</term><term>Modèles moléculaires</term><term>Mutagenèse dirigée</term><term>Peptides (métabolisme)</term><term>Phénomènes biophysiques</term><term>Plasmides</term><term>Protéines recombinantes (isolement et purification)</term><term>Protéines recombinantes (métabolisme)</term><term>Spectrométrie de fluorescence</term><term>Structure quaternaire des protéines</term><term>Structure tertiaire des protéines</term><term>Substances tampon</term><term>Virus du SRAS (enzymologie)</term><term>Électricité statique</term></keywords><keywords scheme="MESH" 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Tertiary</term><term>Spectrometry, Fluorescence</term><term>Static Electricity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biophysique</term><term>Chromatographie en phase liquide à haute performance</term><term>Chromatographie sur gel</term><term>Cinétique</term><term>Concentration en ions d'hydrogène</term><term>Concentration osmolaire</term><term>Cristallographie aux rayons X</term><term>Dichroïsme circulaire</term><term>Dimérisation</term><term>Endopeptidases</term><term>Interactions hydrophobes et hydrophiles</term><term>Liaison hydrogène</term><term>Modèles moléculaires</term><term>Mutagenèse dirigée</term><term>Phénomènes biophysiques</term><term>Plasmides</term><term>Spectrométrie de fluorescence</term><term>Structure quaternaire des protéines</term><term>Structure tertiaire des protéines</term><term>Substances tampon</term><term>Électricité statique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">SARS (severe acute respiratory syndrome) has been one of the most severe viral infectious diseases last year and still remains as a highly risky public health problem around the world. Exploring the types of interactions responsible for structural stabilities of its component protein molecules constitutes one of the approaches to find a destabilization method for the virion particle. In this study, we performed a series of experiments to characterize the quaternary structure of the dimeric coronavirus main protease (M(pro), 3CL(pro)). By using the analytical ultracentrifuge, we demonstrated that the dimeric SARS coronavirus main protease exists as the major form in solution at protein concentration as low as 0.10 mg/mL at neutral pH. The enzyme started to dissociate at acidic and alkali pH values. Ionic strength has profound effect on the dimer stability indicating that the major force involved in the subunit association is ionic interactions. The effect of ionic strength on the protease molecule was reflected by the drastic change of electrostatic potential contour of the enzyme in the presence of NaCl. Analysis of the crystal structures indicated that the interfacial ionic interaction was attributed to the Arg-4...Glu-290 ion pair between the subunits. Detailed examination of the dimer-monomer equilibrium at different pH values reveals apparent pK(a) values of 8.0 +/- 0.2 and 5.0 +/- 0.1 for the Arg-4 and Glu-290, respectively. Mutation at these two positions reduces the association affinity between subunits, and the Glu-290 mutants had diminished enzyme activity. This information is useful in searching for substances that can intervene in the subunit association, which is attractive as a target to neutralize the virulence of SARS coronavirus.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15554703</PMID><DateCompleted><Year>2005</Year><Month>01</Month><Day>11</Day></DateCompleted><DateRevised><Year>2010</Year><Month>11</Month><Day>18</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>43</Volume><Issue>47</Issue><PubDate><Year>2004</Year><Month>Nov</Month><Day>30</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Quaternary structure of the severe acute respiratory syndrome (SARS) coronavirus main protease.</ArticleTitle><Pagination><MedlinePgn>14958-70</MedlinePgn></Pagination><Abstract><AbstractText>SARS (severe acute respiratory syndrome) has been one of the most severe viral infectious diseases last year and still remains as a highly risky public health problem around the world. Exploring the types of interactions responsible for structural stabilities of its component protein molecules constitutes one of the approaches to find a destabilization method for the virion particle. In this study, we performed a series of experiments to characterize the quaternary structure of the dimeric coronavirus main protease (M(pro), 3CL(pro)). By using the analytical ultracentrifuge, we demonstrated that the dimeric SARS coronavirus main protease exists as the major form in solution at protein concentration as low as 0.10 mg/mL at neutral pH. The enzyme started to dissociate at acidic and alkali pH values. Ionic strength has profound effect on the dimer stability indicating that the major force involved in the subunit association is ionic interactions. The effect of ionic strength on the protease molecule was reflected by the drastic change of electrostatic potential contour of the enzyme in the presence of NaCl. Analysis of the crystal structures indicated that the interfacial ionic interaction was attributed to the Arg-4...Glu-290 ion pair between the subunits. Detailed examination of the dimer-monomer equilibrium at different pH values reveals apparent pK(a) values of 8.0 +/- 0.2 and 5.0 +/- 0.1 for the Arg-4 and Glu-290, respectively. Mutation at these two positions reduces the association affinity between subunits, and the Glu-290 mutants had diminished enzyme activity. This information is useful in searching for substances that can intervene in the subunit association, which is attractive as a target to neutralize the virulence of SARS coronavirus.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chou</LastName><ForeName>Chi-Yuan</ForeName><Initials>CY</Initials><AffiliationInfo><Affiliation>Graduate Institute of Life Sciences, National Defense Medical Center, Taipei, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chang</LastName><ForeName>Hui-Chuan</ForeName><Initials>HC</Initials></Author><Author ValidYN="Y"><LastName>Hsu</LastName><ForeName>Wen-Chi</ForeName><Initials>WC</Initials></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>Tien-Zheng</ForeName><Initials>TZ</Initials></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>Chao-Hsiung</ForeName><Initials>CH</Initials></Author><Author ValidYN="Y"><LastName>Chang</LastName><ForeName>Gu-Gang</ForeName><Initials>GG</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002021">Buffers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D010450">Endopeptidases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D055592" MajorTopicYN="N">Biophysical Phenomena</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001703" MajorTopicYN="N">Biophysics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002021" MajorTopicYN="N">Buffers</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002850" MajorTopicYN="N">Chromatography, Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010450" MajorTopicYN="N">Endopeptidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006860" MajorTopicYN="N">Hydrogen Bonding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057927" MajorTopicYN="N">Hydrophobic and Hydrophilic Interactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009994" MajorTopicYN="N">Osmolar Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010957" MajorTopicYN="N">Plasmids</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020836" MajorTopicYN="Y">Protein Structure, Quaternary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013050" MajorTopicYN="N">Spectrometry, Fluorescence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055672" MajorTopicYN="N">Static Electricity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>11</Month><Day>24</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>1</Month><Day>12</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>11</Month><Day>24</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15554703</ArticleId><ArticleId IdType="doi">10.1021/bi0490237</ArticleId></ArticleIdList></PubmedData></pubmed><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="Hsu, Wen Chi" sort="Hsu, Wen Chi" uniqKey="Hsu W" first="Wen-Chi" last="Hsu">Wen-Chi Hsu</name><name sortKey="Lin, Chao Hsiung" sort="Lin, Chao Hsiung" uniqKey="Lin C" first="Chao-Hsiung" last="Lin">Chao-Hsiung Lin</name><name sortKey="Lin, Tien Zheng" sort="Lin, Tien Zheng" uniqKey="Lin T" first="Tien-Zheng" last="Lin">Tien-Zheng Lin</name></noCountry><country name="Taïwan"><noRegion><name sortKey="Chou, Chi Yuan" sort="Chou, Chi Yuan" uniqKey="Chou C" first="Chi-Yuan" last="Chou">Chi-Yuan Chou</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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