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Titolo:
NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: Implications for the enzymatic mechanism
Autore:
Nordstrand, K; Aslund, F; Holmgren, A; Otting, G; Berndt, KD;
Indirizzi:
Karolinska Inst, Dept Med Biochem & Biophys, S-17177 Stockholm, Sweden Karolinska Inst Stockholm Sweden S-17177 phys, S-17177 Stockholm, Sweden Karolinska Inst, Med Nobel Inst Biochem, S-17177 Stockholm, Sweden Karolinska Inst Stockholm Sweden S-17177 chem, S-17177 Stockholm, Sweden
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 2, volume: 286, anno: 1999,
pagine: 541 - 552
SICI:
0022-2836(19990219)286:2<541:NSOECG>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; NUCLEAR-MAGNETIC-RESONANCE; GLUTATHIONE-DEPENDENT SYNTHESIS; FUNCTIONAL-CHARACTERIZATION; RIBONUCLEOTIDE REDUCTASE; 3-DIMENSIONAL STRUCTURE; SECONDARY STRUCTURE; HUMAN THIOREDOXIN; HYDROGEN DONOR; PROTEIN;
Keywords:
glutaredoxin; glutathione; thioredoxin superfamily; NMR structure; thiol-disulfide oxidoreductase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Berndt, KD Karolinska157st, NOVUM, Dept Biosci, Ctr Struct Biochem, Halsovagen 7, S-14 Karolinska Inst Halsovagen 7 Huddinge Sweden S-14157 n 7, S-14
Citazione:
K. Nordstrand et al., "NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: Implications for the enzymatic mechanism", J MOL BIOL, 286(2), 1999, pp. 541-552

Abstract

Glutaredoxins (Grxs) catalyze reversible oxidation/reduction of protein disulfide groups and glutathione-containing mixed disulfide groups via an active site Grx-glutathione mixed disulfide (Grx-SG) intermediate. The NMR solution structure of the Escherichia coli Grx3 mixed disulfide with glutathione (Grx3-SG) was determined using a C14S mutant which traps this intermediate in the redox reaction. The structure contains a thioredoxin fold, with awell-defined binding site for glutathione which involves two intermolecular backbone-backbone hydrogen bonds forming an antiparallel intermolecular beta-bridge between the protein and glutathione. The solution structure of E. coli Grx3-SG also suggests a binding site for a second glutathione in thereduction of the Grx3-SG intermediate, which is consistent with the specificity of reduction observed in Grxs. Molecular details of the structure in relation to the stability of the intermediate and the activity of Grx3 as areductant of glutathione mixed disulfide groups are discussed. A comparison of glutathione binding in Grx3-SG and ligand binding in other members of the thioredoxin superfamily is presented, which illustrates the highly conserved intermolecular interactions in this protein family. (C) 1999 AcademicPress.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 13:34:25