Structural analysis of glutaredoxin domain of Mus musculus thioredoxin glutathione reductase.
Identifieur interne : 000810 ( Main/Exploration ); précédent : 000809; suivant : 000811Structural analysis of glutaredoxin domain of Mus musculus thioredoxin glutathione reductase.
Auteurs : Olena Dobrovolska [Norvège] ; Elena Shumilina ; Vadim N. Gladyshev ; Alexander DikiySource :
- PloS one [ 1932-6203 ] ; 2012.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Complexes multienzymatiques (composition chimique), Complexes multienzymatiques (métabolisme), Conformation des protéines (MeSH), Modèles moléculaires (MeSH), NADH, NADPH oxidoreductases (composition chimique), NADH, NADPH oxidoreductases (métabolisme), Souris (MeSH), Spectroscopie par résonance magnétique (MeSH).
- MESH :
- composition chimique : Complexes multienzymatiques, NADH, NADPH oxidoreductases.
- métabolisme : Complexes multienzymatiques, NADH, NADPH oxidoreductases.
- Animaux, Conformation des protéines, Modèles moléculaires, Souris, Spectroscopie par résonance magnétique.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Multienzyme Complexes, NADH, NADPH Oxidoreductases.
- chemical , metabolism : Multienzyme Complexes, NADH, NADPH Oxidoreductases.
- Animals, Magnetic Resonance Spectroscopy, Mice, Models, Molecular, Protein Conformation.
Abstract
Thioredoxin glutathione reductase (TGR) is a member of the mammalian thioredoxin reductase family that has a monothiol glutaredoxin (Grx) domain attached to the thioredoxin reductase module. Here, we report a structure of the Grx domain of mouse TGR, determined through high resolution NMR spectroscopy to the final backbone RMSD value of 0.48 ± 0.10 Å. The structure represents a sandwich-like molecule composed of a four stranded β-sheet flanked by five α-helixes, with the CxxS active motif located on the catalytic loop. We structurally characterized the glutathione-binding site in the protein and describe sequence and structural relationships of the domain with glutaredoxins. The structure illuminates a key functional center that evolved in mammalian TGRs to act in thiol-disulfide reactions. Our study allows us to hypothesize that Cys105 might be functionally relevant for TGR catalysis. In addition, the data suggest that the N-terminus of Grx acts as a possible regulatory signal also protecting the protein active site from unwanted interactions in cellular cytosol.
DOI: 10.1371/journal.pone.0052914
PubMed: 23300818
PubMed Central: PMC3530482
Affiliations:
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Here, we report a structure of the Grx domain of mouse TGR, determined through high resolution NMR spectroscopy to the final backbone RMSD value of 0.48 ± 0.10 Å. The structure represents a sandwich-like molecule composed of a four stranded β-sheet flanked by five α-helixes, with the CxxS active motif located on the catalytic loop. We structurally characterized the glutathione-binding site in the protein and describe sequence and structural relationships of the domain with glutaredoxins. The structure illuminates a key functional center that evolved in mammalian TGRs to act in thiol-disulfide reactions. Our study allows us to hypothesize that Cys105 might be functionally relevant for TGR catalysis. In addition, the data suggest that the N-terminus of Grx acts as a possible regulatory signal also protecting the protein active site from unwanted interactions in cellular cytosol.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23300818</PMID><DateCompleted><Year>2013</Year><Month>06</Month><Day>24</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>7</Volume><Issue>12</Issue><PubDate><Year>2012</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Structural analysis of glutaredoxin domain of Mus musculus thioredoxin glutathione reductase.</ArticleTitle><Pagination><MedlinePgn>e52914</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0052914</ELocationID><Abstract><AbstractText>Thioredoxin glutathione reductase (TGR) is a member of the mammalian thioredoxin reductase family that has a monothiol glutaredoxin (Grx) domain attached to the thioredoxin reductase module. Here, we report a structure of the Grx domain of mouse TGR, determined through high resolution NMR spectroscopy to the final backbone RMSD value of 0.48 ± 0.10 Å. The structure represents a sandwich-like molecule composed of a four stranded β-sheet flanked by five α-helixes, with the CxxS active motif located on the catalytic loop. We structurally characterized the glutathione-binding site in the protein and describe sequence and structural relationships of the domain with glutaredoxins. The structure illuminates a key functional center that evolved in mammalian TGRs to act in thiol-disulfide reactions. Our study allows us to hypothesize that Cys105 might be functionally relevant for TGR catalysis. 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Gladyshev</name><name sortKey="Shumilina, Elena" sort="Shumilina, Elena" uniqKey="Shumilina E" first="Elena" last="Shumilina">Elena Shumilina</name></noCountry><country name="Norvège"><region name="Trøndelag"><name sortKey="Dobrovolska, Olena" sort="Dobrovolska, Olena" uniqKey="Dobrovolska O" first="Olena" last="Dobrovolska">Olena Dobrovolska</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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