Evidence for the dimerization-mediated catalysis of methionine sulfoxide reductase A from Clostridium oremlandii.
Identifieur interne : 000561 ( Main/Exploration ); précédent : 000560; suivant : 000562Evidence for the dimerization-mediated catalysis of methionine sulfoxide reductase A from Clostridium oremlandii.
Auteurs : Eun Hye Lee [Corée du Sud] ; Kitaik Lee [Corée du Sud] ; Geun-Hee Kwak [Corée du Sud] ; Yeon Seung Park [Corée du Sud] ; Kong-Joo Lee [Corée du Sud] ; Kwang Yeon Hwang [Corée du Sud] ; Hwa-Young Kim [Corée du Sud]Source :
- PloS one [ 1932-6203 ] ; 2015.
Descripteurs français
- KwdFr :
- Algorithmes (MeSH), Catalyse (MeSH), Clostridium (enzymologie), Cristallographie aux rayons X (MeSH), Disulfures (composition chimique), Glutarédoxines (composition chimique), Methionine Sulfoxide Reductases (métabolisme), Modèles moléculaires (MeSH), Multimérisation de protéines (MeSH), Oxydoréduction (MeSH), Spectrométrie de masse (MeSH), Sélénocystéine (métabolisme), Sélénoprotéines (métabolisme).
- MESH :
- composition chimique : Disulfures, Glutarédoxines.
- enzymologie : Clostridium.
- métabolisme : Methionine Sulfoxide Reductases, Sélénocystéine, Sélénoprotéines.
- Algorithmes, Catalyse, Cristallographie aux rayons X, Modèles moléculaires, Multimérisation de protéines, Oxydoréduction, Spectrométrie de masse.
English descriptors
- KwdEn :
- Algorithms (MeSH), Catalysis (MeSH), Clostridium (enzymology), Crystallography, X-Ray (MeSH), Disulfides (chemistry), Glutaredoxins (chemistry), Mass Spectrometry (MeSH), Methionine Sulfoxide Reductases (metabolism), Models, Molecular (MeSH), Oxidation-Reduction (MeSH), Protein Multimerization (MeSH), Selenocysteine (metabolism), Selenoproteins (metabolism).
- MESH :
- chemical , chemistry : Disulfides, Glutaredoxins.
- enzymology : Clostridium.
- chemical , metabolism : Methionine Sulfoxide Reductases, Selenocysteine, Selenoproteins.
- Algorithms, Catalysis, Crystallography, X-Ray, Mass Spectrometry, Models, Molecular, Oxidation-Reduction, Protein Multimerization.
Abstract
Clostridium oremlandii MsrA (CoMsrA) is a natively selenocysteine-containing methionine-S-sulfoxide reductase and classified into a 1-Cys type MsrA. CoMsrA exists as a monomer in solution. Herein, we report evidence that CoMsrA can undergo homodimerization during catalysis. The monomeric CoMsrA dimerizes in the presence of its substrate methionine sulfoxide via an intermolecular disulfide bond between catalytic Cys16 residues. The dimeric CoMsrA is resolved by the reductant glutaredoxin, suggesting the relevance of dimerization in catalysis. The dimerization reaction occurs in a concentration- and time-dependent manner. In addition, the occurrence of homodimer formation in the native selenoprotein CoMsrA is confirmed. We also determine the crystal structure of the dimeric CoMsrA, having the dimer interface around the two catalytic Cys16 residues. A central cone-shaped hole is present in the surface model of dimeric structure, and the two Cys16 residues constitute the base of the hole. Collectively, our biochemical and structural analyses suggest a novel dimerization-mediated mechanism for CoMsrA catalysis that is additionally involved in CoMsrA regeneration by glutaredoxin.
DOI: 10.1371/journal.pone.0131523
PubMed: 26107511
PubMed Central: PMC4479559
Affiliations:
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type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Algorithms (MeSH)</term><term>Catalysis (MeSH)</term><term>Clostridium (enzymology)</term><term>Crystallography, X-Ray (MeSH)</term><term>Disulfides (chemistry)</term><term>Glutaredoxins (chemistry)</term><term>Mass Spectrometry (MeSH)</term><term>Methionine Sulfoxide Reductases (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Protein Multimerization (MeSH)</term><term>Selenocysteine (metabolism)</term><term>Selenoproteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Algorithmes (MeSH)</term><term>Catalyse (MeSH)</term><term>Clostridium (enzymologie)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Disulfures (composition chimique)</term><term>Glutarédoxines (composition chimique)</term><term>Methionine Sulfoxide Reductases (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Multimérisation de protéines (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Spectrométrie de masse (MeSH)</term><term>Sélénocystéine (métabolisme)</term><term>Sélénoprotéines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Disulfides</term><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Disulfures</term><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Clostridium</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Clostridium</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Methionine Sulfoxide Reductases</term><term>Selenocysteine</term><term>Selenoproteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Methionine Sulfoxide Reductases</term><term>Sélénocystéine</term><term>Sélénoprotéines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Algorithms</term><term>Catalysis</term><term>Crystallography, X-Ray</term><term>Mass Spectrometry</term><term>Models, Molecular</term><term>Oxidation-Reduction</term><term>Protein Multimerization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Algorithmes</term><term>Catalyse</term><term>Cristallographie aux rayons X</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Oxydoréduction</term><term>Spectrométrie de masse</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Clostridium oremlandii MsrA (CoMsrA) is a natively selenocysteine-containing methionine-S-sulfoxide reductase and classified into a 1-Cys type MsrA. CoMsrA exists as a monomer in solution. Herein, we report evidence that CoMsrA can undergo homodimerization during catalysis. The monomeric CoMsrA dimerizes in the presence of its substrate methionine sulfoxide via an intermolecular disulfide bond between catalytic Cys16 residues. The dimeric CoMsrA is resolved by the reductant glutaredoxin, suggesting the relevance of dimerization in catalysis. The dimerization reaction occurs in a concentration- and time-dependent manner. In addition, the occurrence of homodimer formation in the native selenoprotein CoMsrA is confirmed. We also determine the crystal structure of the dimeric CoMsrA, having the dimer interface around the two catalytic Cys16 residues. A central cone-shaped hole is present in the surface model of dimeric structure, and the two Cys16 residues constitute the base of the hole. Collectively, our biochemical and structural analyses suggest a novel dimerization-mediated mechanism for CoMsrA catalysis that is additionally involved in CoMsrA regeneration by glutaredoxin. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26107511</PMID><DateCompleted><Year>2016</Year><Month>04</Month><Day>26</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>10</Volume><Issue>6</Issue><PubDate><Year>2015</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Evidence for the dimerization-mediated catalysis of methionine sulfoxide reductase A from Clostridium oremlandii.</ArticleTitle><Pagination><MedlinePgn>e0131523</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0131523</ELocationID><Abstract><AbstractText>Clostridium oremlandii MsrA (CoMsrA) is a natively selenocysteine-containing methionine-S-sulfoxide reductase and classified into a 1-Cys type MsrA. CoMsrA exists as a monomer in solution. Herein, we report evidence that CoMsrA can undergo homodimerization during catalysis. The monomeric CoMsrA dimerizes in the presence of its substrate methionine sulfoxide via an intermolecular disulfide bond between catalytic Cys16 residues. The dimeric CoMsrA is resolved by the reductant glutaredoxin, suggesting the relevance of dimerization in catalysis. The dimerization reaction occurs in a concentration- and time-dependent manner. In addition, the occurrence of homodimer formation in the native selenoprotein CoMsrA is confirmed. We also determine the crystal structure of the dimeric CoMsrA, having the dimer interface around the two catalytic Cys16 residues. A central cone-shaped hole is present in the surface model of dimeric structure, and the two Cys16 residues constitute the base of the hole. Collectively, our biochemical and structural analyses suggest a novel dimerization-mediated mechanism for CoMsrA catalysis that is additionally involved in CoMsrA regeneration by glutaredoxin. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Eun Hye</ForeName><Initials>EH</Initials><AffiliationInfo><Affiliation>Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Kitaik</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kwak</LastName><ForeName>Geun-Hee</ForeName><Initials>GH</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Yeungnam University College of Medicine, Daegu 705-717, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Park</LastName><ForeName>Yeon Seung</ForeName><Initials>YS</Initials><AffiliationInfo><Affiliation>Graduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul 120-750, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Kong-Joo</ForeName><Initials>KJ</Initials><AffiliationInfo><Affiliation>Graduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul 120-750, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hwang</LastName><ForeName>Kwang Yeon</ForeName><Initials>KY</Initials><AffiliationInfo><Affiliation>Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Hwa-Young</ForeName><Initials>HY</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Yeungnam University College of Medicine, Daegu 705-717, Republic of Korea.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>06</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051140">Selenoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0CH9049VIS</RegistryNumber><NameOfSubstance UI="D017279">Selenocysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.-</RegistryNumber><NameOfSubstance UI="D051150">Methionine Sulfoxide Reductases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000465" MajorTopicYN="N">Algorithms</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003013" MajorTopicYN="N">Clostridium</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051150" MajorTopicYN="N">Methionine Sulfoxide Reductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein 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Lee</name></region><name sortKey="Hwang, Kwang Yeon" sort="Hwang, Kwang Yeon" uniqKey="Hwang K" first="Kwang Yeon" last="Hwang">Kwang Yeon Hwang</name><name sortKey="Kim, Hwa Young" sort="Kim, Hwa Young" uniqKey="Kim H" first="Hwa-Young" last="Kim">Hwa-Young Kim</name><name sortKey="Kwak, Geun Hee" sort="Kwak, Geun Hee" uniqKey="Kwak G" first="Geun-Hee" last="Kwak">Geun-Hee Kwak</name><name sortKey="Lee, Kitaik" sort="Lee, Kitaik" uniqKey="Lee K" first="Kitaik" last="Lee">Kitaik Lee</name><name sortKey="Lee, Kong Joo" sort="Lee, Kong Joo" uniqKey="Lee K" first="Kong-Joo" last="Lee">Kong-Joo Lee</name><name sortKey="Park, Yeon Seung" sort="Park, Yeon Seung" uniqKey="Park Y" first="Yeon Seung" last="Park">Yeon Seung Park</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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