Secondary structure and fold homology of the ArsC protein from the Escherichia coli arsenic resistance plasmid R773.
Identifieur interne : 001091 ( Main/Exploration ); précédent : 001090; suivant : 001092Secondary structure and fold homology of the ArsC protein from the Escherichia coli arsenic resistance plasmid R773.
Auteurs : S Y Stevens [États-Unis] ; W. Hu ; T. Gladysheva ; B P Rosen ; E R Zuiderweg ; L. LeeSource :
- Biochemistry [ 0006-2960 ] ; 1999.
Descripteurs français
- KwdFr :
- Adenosine triphosphatases (composition chimique), Adenosine triphosphatases (génétique), Arsenic (pharmacologie), Arsenite Transporting ATPases (MeSH), Complexes multienzymatiques (MeSH), Données de séquences moléculaires (MeSH), Escherichia coli (composition chimique), Escherichia coli (génétique), Oxydoréduction (MeSH), Plasmides (composition chimique), Plasmides (génétique), Pliage des protéines (MeSH), Pompes ioniques (MeSH), Résistance microbienne aux médicaments (génétique), Résonance magnétique nucléaire biomoléculaire (MeSH), Similitude de séquences d'acides aminés (MeSH), Sites de fixation (MeSH), Structure secondaire des protéines (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Adenosine triphosphatases, Escherichia coli, Plasmides.
- génétique : Adenosine triphosphatases, Escherichia coli, Plasmides, Résistance microbienne aux médicaments.
- pharmacologie : Arsenic.
- Arsenite Transporting ATPases, Complexes multienzymatiques, Données de séquences moléculaires, Oxydoréduction, Pliage des protéines, Pompes ioniques, Résonance magnétique nucléaire biomoléculaire, Similitude de séquences d'acides aminés, Sites de fixation, Structure secondaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Adenosine Triphosphatases (chemistry), Adenosine Triphosphatases (genetics), Amino Acid Sequence (MeSH), Arsenic (pharmacology), Arsenite Transporting ATPases (MeSH), Binding Sites (MeSH), Drug Resistance, Microbial (genetics), Escherichia coli (chemistry), Escherichia coli (genetics), Ion Pumps (MeSH), Molecular Sequence Data (MeSH), Multienzyme Complexes (MeSH), Nuclear Magnetic Resonance, Biomolecular (MeSH), Oxidation-Reduction (MeSH), Plasmids (chemistry), Plasmids (genetics), Protein Folding (MeSH), Protein Structure, Secondary (MeSH), Sequence Homology, Amino Acid (MeSH).
- MESH :
- chemical , chemistry : Adenosine Triphosphatases.
- chemical , genetics : Adenosine Triphosphatases.
- chemical , pharmacology : Arsenic.
- chemistry : Escherichia coli, Plasmids.
- genetics : Drug Resistance, Microbial, Escherichia coli, Plasmids.
- Amino Acid Sequence, Arsenite Transporting ATPases, Binding Sites, Ion Pumps, Molecular Sequence Data, Multienzyme Complexes, Nuclear Magnetic Resonance, Biomolecular, Oxidation-Reduction, Protein Folding, Protein Structure, Secondary, Sequence Homology, Amino Acid.
Abstract
Resistance to several toxic anions in Escherichia coli is conferred by the ars operon carried on plasmid R773. The gene products of this operon catalyze extrusion of antimonials and arsenicals from cells. In this paper, we report the determination of the overall fold for ArsC, a 16 kDa protein of the ars operon involved in the reduction of arsenate to arsenite, using multidimensional, multinuclear NMR. The protein is found to contain large regions of extensive mobility, particularly in the active site. A model fold, computed on the basis of a preliminary set of NOEs, was found to be structurally homologous to E. coli glutaredoxin, thiol transferases, and glutathione S-transferase. Some kinship to the structure of low molecular weight tyrosine phosphatases, based on rough topological similarity but more so on the basis of a common anion-binding-loop motif H-CX(n)R, was also detected. Although functional, secondary, and tertiary structural homology is observed with these molecules, no significant homology in primary structure was detected. The mobilities of the active site of ArsC and of other enzymes are discussed.
DOI: 10.1021/bi990333c
PubMed: 10433726
Affiliations:
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Le document en format XML
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The gene products of this operon catalyze extrusion of antimonials and arsenicals from cells. In this paper, we report the determination of the overall fold for ArsC, a 16 kDa protein of the ars operon involved in the reduction of arsenate to arsenite, using multidimensional, multinuclear NMR. The protein is found to contain large regions of extensive mobility, particularly in the active site. A model fold, computed on the basis of a preliminary set of NOEs, was found to be structurally homologous to E. coli glutaredoxin, thiol transferases, and glutathione S-transferase. Some kinship to the structure of low molecular weight tyrosine phosphatases, based on rough topological similarity but more so on the basis of a common anion-binding-loop motif H-CX(n)R, was also detected. Although functional, secondary, and tertiary structural homology is observed with these molecules, no significant homology in primary structure was detected. The mobilities of the active site of ArsC and of other enzymes are discussed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10433726</PMID><DateCompleted><Year>1999</Year><Month>09</Month><Day>03</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>38</Volume><Issue>31</Issue><PubDate><Year>1999</Year><Month>Aug</Month><Day>03</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Secondary structure and fold homology of the ArsC protein from the Escherichia coli arsenic resistance plasmid R773.</ArticleTitle><Pagination><MedlinePgn>10178-86</MedlinePgn></Pagination><Abstract><AbstractText>Resistance to several toxic anions in Escherichia coli is conferred by the ars operon carried on plasmid R773. The gene products of this operon catalyze extrusion of antimonials and arsenicals from cells. In this paper, we report the determination of the overall fold for ArsC, a 16 kDa protein of the ars operon involved in the reduction of arsenate to arsenite, using multidimensional, multinuclear NMR. The protein is found to contain large regions of extensive mobility, particularly in the active site. A model fold, computed on the basis of a preliminary set of NOEs, was found to be structurally homologous to E. coli glutaredoxin, thiol transferases, and glutathione S-transferase. Some kinship to the structure of low molecular weight tyrosine phosphatases, based on rough topological similarity but more so on the basis of a common anion-binding-loop motif H-CX(n)R, was also detected. Although functional, secondary, and tertiary structural homology is observed with these molecules, no significant homology in primary structure was detected. The mobilities of the active site of ArsC and of other enzymes are discussed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Stevens</LastName><ForeName>S Y</ForeName><Initials>SY</Initials><AffiliationInfo><Affiliation>Biophysics Research Division, Department of Biological Chemistry, University of Michigan, Ann Arbor 48109-1055, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hu</LastName><ForeName>W</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Gladysheva</LastName><ForeName>T</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Rosen</LastName><ForeName>B P</ForeName><Initials>BP</Initials></Author><Author ValidYN="Y"><LastName>Zuiderweg</LastName><ForeName>E R</ForeName><Initials>ER</Initials></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>L</ForeName><Initials>L</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>5R01 GM52406</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM 52216</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</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="D016623">Ion Pumps</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009097">Multienzyme Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="D000251">Adenosine Triphosphatases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.3.16</RegistryNumber><NameOfSubstance UI="D053501">Arsenite Transporting ATPases</NameOfSubstance></Chemical><Chemical><RegistryNumber>N712M78A8G</RegistryNumber><NameOfSubstance UI="D001151">Arsenic</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000251" MajorTopicYN="N">Adenosine Triphosphatases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001151" MajorTopicYN="N">Arsenic</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053501" MajorTopicYN="N">Arsenite Transporting ATPases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004352" MajorTopicYN="N">Drug Resistance, Microbial</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016623" MajorTopicYN="Y">Ion Pumps</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009097" MajorTopicYN="Y">Multienzyme Complexes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019906" MajorTopicYN="N">Nuclear Magnetic Resonance, Biomolecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010957" MajorTopicYN="N">Plasmids</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="Y">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="Y">Sequence Homology, Amino Acid</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year><Month>8</Month><Day>6</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>8</Month><Day>6</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>8</Month><Day>6</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10433726</ArticleId><ArticleId IdType="doi">10.1021/bi990333c</ArticleId><ArticleId IdType="pii">bi990333c</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Gladysheva, T" sort="Gladysheva, T" uniqKey="Gladysheva T" first="T" last="Gladysheva">T. Gladysheva</name><name sortKey="Hu, W" sort="Hu, W" uniqKey="Hu W" first="W" last="Hu">W. Hu</name><name sortKey="Lee, L" sort="Lee, L" uniqKey="Lee L" first="L" last="Lee">L. Lee</name><name sortKey="Rosen, B P" sort="Rosen, B P" uniqKey="Rosen B" first="B P" last="Rosen">B P Rosen</name><name sortKey="Zuiderweg, E R" sort="Zuiderweg, E R" uniqKey="Zuiderweg E" first="E R" last="Zuiderweg">E R Zuiderweg</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Stevens, S Y" sort="Stevens, S Y" uniqKey="Stevens S" first="S Y" last="Stevens">S Y Stevens</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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