Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli.
Identifieur interne : 001056 ( Main/Exploration ); précédent : 001055; suivant : 001057Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli.
Auteurs : R A Fabianek [Suisse] ; H. Hennecke ; L. Thöny-MeyerSource :
- FEMS microbiology reviews [ 0168-6445 ] ; 2000.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Protein-disulfide reductase (glutathione).
- enzymologie : Escherichia coli, Périplasme.
- métabolisme : Protein-disulfide reductase (glutathione).
- Données de séquences moléculaires, Oxydoréduction, Séquence d'acides aminés.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Protein Disulfide Reductase (Glutathione).
- enzymology : Escherichia coli, Periplasm.
- chemical , metabolism : Protein Disulfide Reductase (Glutathione).
- Amino Acid Sequence, Molecular Sequence Data, Oxidation-Reduction.
Abstract
Disulfide bond formation is part of the folding pathway for many periplasmic and outer membrane proteins that contain structural disulfide bonds. In Escherichia coli, a broad variety of periplasmic protein thiol:disulfide oxidoreductases have been identified in recent years, which substantially contribute to this pathway. Like the well-known cytoplasmic thioredoxins and glutaredoxins, these periplasmic protein thiol:disulfide oxidoreductases contain the conserved C-X-X-C motif in their active site. Most of them have a domain that displays the thioredoxin-like fold. In contrast to the cytoplasmic system, which consists exclusively of reducing proteins, the periplasmic oxidoreductases have either an oxidising, a reducing or an isomerisation activity. Apart from understanding their physiological role, it is of interest to learn how these proteins interact with their target molecules and how they are recycled as electron donors or acceptors. This review reflects the recently made efforts to elucidate the sources of oxidising and reducing power in the periplasm as well as the different properties of certain periplasmic protein thiol:disulfide oxidoreductases of E. coli.
DOI: 10.1111/j.1574-6976.2000.tb00544.x
PubMed: 10841975
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli.</title><author><name sortKey="Fabianek, R A" sort="Fabianek, R A" uniqKey="Fabianek R" first="R A" last="Fabianek">R A Fabianek</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Microbiology, Swiss Federal Institute of Technology, ETH-Zentrum, CH-8092, Zurich, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Institute of Microbiology, Swiss Federal Institute of Technology, ETH-Zentrum, CH-8092, Zurich</wicri:regionArea><wicri:noRegion>Zurich</wicri:noRegion></affiliation></author><author><name sortKey="Hennecke, H" sort="Hennecke, H" uniqKey="Hennecke H" first="H" last="Hennecke">H. Hennecke</name></author><author><name sortKey="Thony Meyer, L" sort="Thony Meyer, L" uniqKey="Thony Meyer L" first="L" last="Thöny-Meyer">L. Thöny-Meyer</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2000">2000</date><idno type="RBID">pubmed:10841975</idno><idno type="pmid">10841975</idno><idno type="doi">10.1111/j.1574-6976.2000.tb00544.x</idno><idno type="wicri:Area/Main/Corpus">001072</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001072</idno><idno type="wicri:Area/Main/Curation">001072</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001072</idno><idno type="wicri:Area/Main/Exploration">001072</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli.</title><author><name sortKey="Fabianek, R A" sort="Fabianek, R A" uniqKey="Fabianek R" first="R A" last="Fabianek">R A Fabianek</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Microbiology, Swiss Federal Institute of Technology, ETH-Zentrum, CH-8092, Zurich, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Institute of Microbiology, Swiss Federal Institute of Technology, ETH-Zentrum, CH-8092, Zurich</wicri:regionArea><wicri:noRegion>Zurich</wicri:noRegion></affiliation></author><author><name sortKey="Hennecke, H" sort="Hennecke, H" uniqKey="Hennecke H" first="H" last="Hennecke">H. Hennecke</name></author><author><name sortKey="Thony Meyer, L" sort="Thony Meyer, L" uniqKey="Thony Meyer L" first="L" last="Thöny-Meyer">L. Thöny-Meyer</name></author></analytic><series><title level="j">FEMS microbiology reviews</title><idno type="ISSN">0168-6445</idno><imprint><date when="2000" type="published">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Escherichia coli (enzymology)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Periplasm (enzymology)</term><term>Protein Disulfide Reductase (Glutathione) (chemistry)</term><term>Protein Disulfide Reductase (Glutathione) (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (enzymologie)</term><term>Oxydoréduction (MeSH)</term><term>Protein-disulfide reductase (glutathione) (composition chimique)</term><term>Protein-disulfide reductase (glutathione) (métabolisme)</term><term>Périplasme (enzymologie)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Protein Disulfide Reductase (Glutathione)</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protein-disulfide reductase (glutathione)</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Escherichia coli</term><term>Périplasme</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Escherichia coli</term><term>Periplasm</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Protein Disulfide Reductase (Glutathione)</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protein-disulfide reductase (glutathione)</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Oxydoréduction</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Disulfide bond formation is part of the folding pathway for many periplasmic and outer membrane proteins that contain structural disulfide bonds. In Escherichia coli, a broad variety of periplasmic protein thiol:disulfide oxidoreductases have been identified in recent years, which substantially contribute to this pathway. Like the well-known cytoplasmic thioredoxins and glutaredoxins, these periplasmic protein thiol:disulfide oxidoreductases contain the conserved C-X-X-C motif in their active site. Most of them have a domain that displays the thioredoxin-like fold. In contrast to the cytoplasmic system, which consists exclusively of reducing proteins, the periplasmic oxidoreductases have either an oxidising, a reducing or an isomerisation activity. Apart from understanding their physiological role, it is of interest to learn how these proteins interact with their target molecules and how they are recycled as electron donors or acceptors. This review reflects the recently made efforts to elucidate the sources of oxidising and reducing power in the periplasm as well as the different properties of certain periplasmic protein thiol:disulfide oxidoreductases of E. coli.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10841975</PMID><DateCompleted><Year>2000</Year><Month>08</Month><Day>22</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>30</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0168-6445</ISSN><JournalIssue CitedMedium="Print"><Volume>24</Volume><Issue>3</Issue><PubDate><Year>2000</Year><Month>Jul</Month></PubDate></JournalIssue><Title>FEMS microbiology reviews</Title><ISOAbbreviation>FEMS Microbiol Rev</ISOAbbreviation></Journal><ArticleTitle>Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli.</ArticleTitle><Pagination><MedlinePgn>303-16</MedlinePgn></Pagination><Abstract><AbstractText>Disulfide bond formation is part of the folding pathway for many periplasmic and outer membrane proteins that contain structural disulfide bonds. In Escherichia coli, a broad variety of periplasmic protein thiol:disulfide oxidoreductases have been identified in recent years, which substantially contribute to this pathway. Like the well-known cytoplasmic thioredoxins and glutaredoxins, these periplasmic protein thiol:disulfide oxidoreductases contain the conserved C-X-X-C motif in their active site. Most of them have a domain that displays the thioredoxin-like fold. In contrast to the cytoplasmic system, which consists exclusively of reducing proteins, the periplasmic oxidoreductases have either an oxidising, a reducing or an isomerisation activity. Apart from understanding their physiological role, it is of interest to learn how these proteins interact with their target molecules and how they are recycled as electron donors or acceptors. This review reflects the recently made efforts to elucidate the sources of oxidising and reducing power in the periplasm as well as the different properties of certain periplasmic protein thiol:disulfide oxidoreductases of E. coli.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fabianek</LastName><ForeName>R A</ForeName><Initials>RA</Initials><AffiliationInfo><Affiliation>Institute of Microbiology, Swiss Federal Institute of Technology, ETH-Zentrum, CH-8092, Zurich, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hennecke</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Thöny-Meyer</LastName><ForeName>L</ForeName><Initials>L</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEMS Microbiol Rev</MedlineTA><NlmUniqueID>8902526</NlmUniqueID><ISSNLinking>0168-6445</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019897" MajorTopicYN="N">Periplasm</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="N">Protein Disulfide Reductase (Glutathione)</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>130</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>6</Month><Day>8</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2000</Year><Month>8</Month><Day>29</Day><Hour>11</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>6</Month><Day>8</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10841975</ArticleId><ArticleId IdType="pii">S0168-6445(00)00028-0</ArticleId><ArticleId IdType="doi">10.1111/j.1574-6976.2000.tb00544.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country></list><tree><noCountry><name sortKey="Hennecke, H" sort="Hennecke, H" uniqKey="Hennecke H" first="H" last="Hennecke">H. Hennecke</name><name sortKey="Thony Meyer, L" sort="Thony Meyer, L" uniqKey="Thony Meyer L" first="L" last="Thöny-Meyer">L. Thöny-Meyer</name></noCountry><country name="Suisse"><noRegion><name sortKey="Fabianek, R A" sort="Fabianek, R A" uniqKey="Fabianek R" first="R A" last="Fabianek">R A Fabianek</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001056 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001056 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= GlutaredoxinV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:10841975
|texte= Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:10841975" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |