Structural and mechanistic aspects of S-S bonds in the thioredoxin-like family of proteins.
Identifieur interne : 000121 ( Main/Exploration ); précédent : 000120; suivant : 000122Structural and mechanistic aspects of S-S bonds in the thioredoxin-like family of proteins.
Auteurs : Sérgio F. Sousa [Portugal] ; Rui P P. Neves [Portugal] ; Sodiq O. Waheed [Portugal] ; Pedro A. Fernandes [Portugal] ; Maria João Ramos [Portugal]Source :
- Biological chemistry [ 1437-4315 ] ; 2019.
Descripteurs français
- KwdFr :
- Disulfures (composition chimique), Disulfures (métabolisme), Glutarédoxines (composition chimique), Glutarédoxines (métabolisme), Humains (MeSH), Modèles moléculaires (MeSH), Protein Disulfide-Isomerases (composition chimique), Protein Disulfide-Isomerases (métabolisme), Thiorédoxines (composition chimique), Thiorédoxines (métabolisme).
- MESH :
- composition chimique : Disulfures, Glutarédoxines, Protein Disulfide-Isomerases, Thiorédoxines.
- métabolisme : Disulfures, Glutarédoxines, Protein Disulfide-Isomerases, Thiorédoxines.
- Humains, Modèles moléculaires.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Disulfides, Glutaredoxins, Protein Disulfide-Isomerases, Thioredoxins.
- chemical , metabolism : Disulfides, Glutaredoxins, Protein Disulfide-Isomerases, Thioredoxins.
- Humans, Models, Molecular.
Abstract
Disulfide bonds play a critical role in a variety of structural and mechanistic processes associated with proteins inside the cells and in the extracellular environment. The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction. Here, we review the structural and mechanistic determinants behind the thiol-disulfide exchange reactions for the different enzyme types within this family, rationalizing the known experimental data in light of the results from computational studies. The analysis sheds new atomic-level insight into the structural and mechanistic variations that characterize the different enzymes in the family, helping to explain the associated functional diversity. Furthermore, we review here a pattern of stabilization/destabilization of the conserved active-site cysteine residues presented beforehand, which is fully consistent with the observed roles played by the thioredoxin family of enzymes.
DOI: 10.1515/hsz-2018-0319
PubMed: 30367780
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Waheed</name><affiliation wicri:level="1"><nlm:affiliation>UCIBIO@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.</nlm:affiliation><country xml:lang="fr">Portugal</country><wicri:regionArea>UCIBIO@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto</wicri:regionArea><wicri:noRegion>4169-007 Porto</wicri:noRegion></affiliation></author><author><name sortKey="Fernandes, Pedro A" sort="Fernandes, Pedro A" uniqKey="Fernandes P" first="Pedro A" last="Fernandes">Pedro A. Fernandes</name><affiliation wicri:level="1"><nlm:affiliation>UCIBIO@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.</nlm:affiliation><country xml:lang="fr">Portugal</country><wicri:regionArea>UCIBIO@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto</wicri:regionArea><wicri:noRegion>4169-007 Porto</wicri:noRegion></affiliation></author><author><name sortKey="Ramos, Maria Joao" sort="Ramos, Maria Joao" uniqKey="Ramos M" first="Maria João" last="Ramos">Maria João Ramos</name><affiliation wicri:level="1"><nlm:affiliation>UCIBIO@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.</nlm:affiliation><country xml:lang="fr">Portugal</country><wicri:regionArea>UCIBIO@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto</wicri:regionArea><wicri:noRegion>4169-007 Porto</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biological chemistry</title><idno type="eISSN">1437-4315</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Disulfides (chemistry)</term><term>Disulfides (metabolism)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (metabolism)</term><term>Humans (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Protein Disulfide-Isomerases (chemistry)</term><term>Protein Disulfide-Isomerases (metabolism)</term><term>Thioredoxins (chemistry)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Disulfures (composition chimique)</term><term>Disulfures (métabolisme)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (métabolisme)</term><term>Humains (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Protein Disulfide-Isomerases (composition chimique)</term><term>Protein Disulfide-Isomerases (métabolisme)</term><term>Thiorédoxines (composition chimique)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Disulfides</term><term>Glutaredoxins</term><term>Protein Disulfide-Isomerases</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Disulfides</term><term>Glutaredoxins</term><term>Protein Disulfide-Isomerases</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Disulfures</term><term>Glutarédoxines</term><term>Protein Disulfide-Isomerases</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Disulfures</term><term>Glutarédoxines</term><term>Protein Disulfide-Isomerases</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Models, Molecular</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Modèles moléculaires</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Disulfide bonds play a critical role in a variety of structural and mechanistic processes associated with proteins inside the cells and in the extracellular environment. The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction. Here, we review the structural and mechanistic determinants behind the thiol-disulfide exchange reactions for the different enzyme types within this family, rationalizing the known experimental data in light of the results from computational studies. The analysis sheds new atomic-level insight into the structural and mechanistic variations that characterize the different enzymes in the family, helping to explain the associated functional diversity. Furthermore, we review here a pattern of stabilization/destabilization of the conserved active-site cysteine residues presented beforehand, which is fully consistent with the observed roles played by the thioredoxin family of enzymes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30367780</PMID><DateCompleted><Year>2019</Year><Month>12</Month><Day>06</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>17</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1437-4315</ISSN><JournalIssue CitedMedium="Internet"><Volume>400</Volume><Issue>5</Issue><PubDate><Year>2019</Year><Month>04</Month><Day>24</Day></PubDate></JournalIssue><Title>Biological chemistry</Title><ISOAbbreviation>Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Structural and mechanistic aspects of S-S bonds in the thioredoxin-like family of proteins.</ArticleTitle><Pagination><MedlinePgn>575-587</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1515/hsz-2018-0319</ELocationID><ELocationID EIdType="pii" ValidYN="Y">/j/bchm.2019.400.issue-5/hsz-2018-0319/hsz-2018-0319.xml</ELocationID><Abstract><AbstractText>Disulfide bonds play a critical role in a variety of structural and mechanistic processes associated with proteins inside the cells and in the extracellular environment. The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction. Here, we review the structural and mechanistic determinants behind the thiol-disulfide exchange reactions for the different enzyme types within this family, rationalizing the known experimental data in light of the results from computational studies. The analysis sheds new atomic-level insight into the structural and mechanistic variations that characterize the different enzymes in the family, helping to explain the associated functional diversity. Furthermore, we review here a pattern of stabilization/destabilization of the conserved active-site cysteine residues presented beforehand, which is fully consistent with the observed roles played by the thioredoxin family of enzymes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sousa</LastName><ForeName>Sérgio F</ForeName><Initials>SF</Initials><AffiliationInfo><Affiliation>UCIBIO@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Neves</LastName><ForeName>Rui P P</ForeName><Initials>RPP</Initials><AffiliationInfo><Affiliation>UCIBIO@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Waheed</LastName><ForeName>Sodiq O</ForeName><Initials>SO</Initials><AffiliationInfo><Affiliation>UCIBIO@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fernandes</LastName><ForeName>Pedro A</ForeName><Initials>PA</Initials><AffiliationInfo><Affiliation>UCIBIO@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ramos</LastName><ForeName>Maria João</ForeName><Initials>MJ</Initials><AffiliationInfo><Affiliation>UCIBIO@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.</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><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Biol Chem</MedlineTA><NlmUniqueID>9700112</NlmUniqueID><ISSNLinking>1431-6730</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516005">GLRX protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C491203">TXN protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 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MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Grx</Keyword><Keyword MajorTopicYN="Y">PDI</Keyword><Keyword MajorTopicYN="Y">Trx</Keyword><Keyword MajorTopicYN="Y">disulfide</Keyword><Keyword MajorTopicYN="Y">pKa</Keyword><Keyword MajorTopicYN="Y">thiol-disulfide exchange</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>07</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>10</Month><Day>22</Day></PubMedPubDate><PubMedPubDate 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Sousa</name></noRegion><name sortKey="Fernandes, Pedro A" sort="Fernandes, Pedro A" uniqKey="Fernandes P" first="Pedro A" last="Fernandes">Pedro A. Fernandes</name><name sortKey="Neves, Rui P P" sort="Neves, Rui P P" uniqKey="Neves R" first="Rui P P" last="Neves">Rui P P. Neves</name><name sortKey="Ramos, Maria Joao" sort="Ramos, Maria Joao" uniqKey="Ramos M" first="Maria João" last="Ramos">Maria João Ramos</name><name sortKey="Waheed, Sodiq O" sort="Waheed, Sodiq O" uniqKey="Waheed S" first="Sodiq O" last="Waheed">Sodiq O. Waheed</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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