The structure of the thioredoxin-triosephosphate isomerase complex provides insights into the reversible glutathione-mediated regulation of triosephosphate isomerase.
Identifieur interne : 000799 ( Main/Exploration ); précédent : 000798; suivant : 000800The structure of the thioredoxin-triosephosphate isomerase complex provides insights into the reversible glutathione-mediated regulation of triosephosphate isomerase.
Auteurs : Hameed M S. Shahul [Inde] ; Siddhartha P. SarmaSource :
- Biochemistry [ 1520-4995 ] ; 2012.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Bovins (MeSH), Cristallographie aux rayons X (MeSH), Glutarédoxines (composition chimique), Glutathion (composition chimique), Glutathion (physiologie), Interactions hydrophobes et hydrophiles (MeSH), Liaison aux protéines (physiologie), Modèles moléculaires (MeSH), Plasmodium falciparum (enzymologie), Protéines Escherichia coli (composition chimique), Protéines Escherichia coli (physiologie), Protéines de protozoaire (composition chimique), Protéines de protozoaire (physiologie), Thiorédoxines (composition chimique), Thiorédoxines (physiologie), Triose phosphate isomerase (composition chimique), Triose phosphate isomerase (métabolisme), Triose phosphate isomerase (physiologie).
- MESH :
- composition chimique : Glutarédoxines, Glutathion, Protéines Escherichia coli, Protéines de protozoaire, Thiorédoxines, Triose phosphate isomerase.
- enzymologie : Plasmodium falciparum.
- métabolisme : Triose phosphate isomerase.
- physiologie : Glutathion, Liaison aux protéines, Protéines Escherichia coli, Protéines de protozoaire, Thiorédoxines, Triose phosphate isomerase.
- Animaux, Bovins, Cristallographie aux rayons X, Interactions hydrophobes et hydrophiles, Modèles moléculaires.
English descriptors
- KwdEn :
- Animals (MeSH), Cattle (MeSH), Crystallography, X-Ray (MeSH), Escherichia coli Proteins (chemistry), Escherichia coli Proteins (physiology), Glutaredoxins (chemistry), Glutathione (chemistry), Glutathione (physiology), Hydrophobic and Hydrophilic Interactions (MeSH), Models, Molecular (MeSH), Plasmodium falciparum (enzymology), Protein Binding (physiology), Protozoan Proteins (chemistry), Protozoan Proteins (physiology), Thioredoxins (chemistry), Thioredoxins (physiology), Triose-Phosphate Isomerase (chemistry), Triose-Phosphate Isomerase (metabolism), Triose-Phosphate Isomerase (physiology).
- MESH :
- chemical , chemistry : Escherichia coli Proteins, Glutaredoxins, Glutathione, Protozoan Proteins, Thioredoxins, Triose-Phosphate Isomerase.
- chemical , metabolism : Triose-Phosphate Isomerase.
- chemical , physiology : Escherichia coli Proteins, Glutathione, Protozoan Proteins, Thioredoxins, Triose-Phosphate Isomerase.
- enzymology : Plasmodium falciparum.
- physiology : Protein Binding.
- Animals, Cattle, Crystallography, X-Ray, Hydrophobic and Hydrophilic Interactions, Models, Molecular.
Abstract
Protein-protein interactions are crucial for many biological functions. The redox interactome encompasses numerous weak transient interactions in which thioredoxin plays a central role. Proteomic studies have shown that thioredoxin binds to numerous proteins belonging to various cellular processes, including energy metabolism. Thioredoxin has cross talk with other redox mechanisms involving glutathionylation and has functional overlap with glutaredoxin in deglutathionylation reactions. In this study, we have explored the structural and biochemical interactions of thioredoxin with the glycolytic enzyme, triosephosphate isomerase. Nuclear magnetic resonance chemical shift mapping methods and molecular dynamics-based docking have been applied in deriving a structural model of the thioredoxin-triosephosphate isomerase complex. The spatial proximity of active site cysteine residues of thioredoxin to reactive thiol groups on triosephosphate isomerase provides a direct link to the observed deglutathionylation of cysteine 217 in triosephosphate isomerase, thereby reversing the inhibitory effect of S-glutathionylation of triosephosphate isomerase.
DOI: 10.1021/bi201224s
PubMed: 22126412
Affiliations:
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Le document en format XML
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The redox interactome encompasses numerous weak transient interactions in which thioredoxin plays a central role. Proteomic studies have shown that thioredoxin binds to numerous proteins belonging to various cellular processes, including energy metabolism. Thioredoxin has cross talk with other redox mechanisms involving glutathionylation and has functional overlap with glutaredoxin in deglutathionylation reactions. In this study, we have explored the structural and biochemical interactions of thioredoxin with the glycolytic enzyme, triosephosphate isomerase. Nuclear magnetic resonance chemical shift mapping methods and molecular dynamics-based docking have been applied in deriving a structural model of the thioredoxin-triosephosphate isomerase complex. The spatial proximity of active site cysteine residues of thioredoxin to reactive thiol groups on triosephosphate isomerase provides a direct link to the observed deglutathionylation of cysteine 217 in triosephosphate isomerase, thereby reversing the inhibitory effect of S-glutathionylation of triosephosphate isomerase.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22126412</PMID><DateCompleted><Year>2012</Year><Month>03</Month><Day>08</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-4995</ISSN><JournalIssue CitedMedium="Internet"><Volume>51</Volume><Issue>1</Issue><PubDate><Year>2012</Year><Month>Jan</Month><Day>10</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>The structure of the thioredoxin-triosephosphate isomerase complex provides insights into the reversible glutathione-mediated regulation of triosephosphate isomerase.</ArticleTitle><Pagination><MedlinePgn>533-44</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/bi201224s</ELocationID><Abstract><AbstractText>Protein-protein interactions are crucial for many biological functions. The redox interactome encompasses numerous weak transient interactions in which thioredoxin plays a central role. Proteomic studies have shown that thioredoxin binds to numerous proteins belonging to various cellular processes, including energy metabolism. Thioredoxin has cross talk with other redox mechanisms involving glutathionylation and has functional overlap with glutaredoxin in deglutathionylation reactions. In this study, we have explored the structural and biochemical interactions of thioredoxin with the glycolytic enzyme, triosephosphate isomerase. Nuclear magnetic resonance chemical shift mapping methods and molecular dynamics-based docking have been applied in deriving a structural model of the thioredoxin-triosephosphate isomerase complex. The spatial proximity of active site cysteine residues of thioredoxin to reactive thiol groups on triosephosphate isomerase provides a direct link to the observed deglutathionylation of cysteine 217 in triosephosphate isomerase, thereby reversing the inhibitory effect of S-glutathionylation of triosephosphate isomerase.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shahul</LastName><ForeName>Hameed M S</ForeName><Initials>HM</Initials><AffiliationInfo><Affiliation>Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, Karnataka, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sarma</LastName><ForeName>Siddhartha P</ForeName><Initials>SP</Initials></Author></AuthorList><Language>eng</Language><DataBankList 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Sarma</name></noCountry><country name="Inde"><noRegion><name sortKey="Shahul, Hameed M S" sort="Shahul, Hameed M S" uniqKey="Shahul H" first="Hameed M S" last="Shahul">Hameed M S. Shahul</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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