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Titolo:
GLUTAREDOXIN-3 FROM ESCHERICHIA-COLI - AMINO-ACID-SEQUENCE, H-1 AND N-15 NMR ASSIGNMENTS, AND STRUCTURAL-ANALYSIS
Autore:
ASLUND F; NORDSTRAND K; BERNDT KD; NIKKOLA M; BERGMAN T; PONSTINGL H; JORNVALL H; OTTING G; HOLMGREN A;
Indirizzi:
KAROLINSKA INST,MED NOBEL INST BIOCHEM,DEPT MED BIOCHEM & BIOPHYS S-17177 STOCKHOLM SWEDEN KAROLINSKA INST,MED NOBEL INST BIOCHEM,DEPT MED BIOCHEM & BIOPHYS S-17177 STOCKHOLM SWEDEN SWEDISH UNIV AGR SCI,CTR BIOMED,DEPT MOLEC BIOL S-75124 UPPSALA SWEDEN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 12, volume: 271, anno: 1996,
pagine: 6736 - 6745
SICI:
0021-9258(1996)271:12<6736:GFE-AH>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
SECONDARY STRUCTURE DETERMINATION; GLUTATHIONE-DEPENDENT SYNTHESIS; PROTON PROTON DISTANCES; 3-DIMENSIONAL STRUCTURE; HUMAN THIOREDOXIN; MIXED DISULFIDE; PROTEINS; SPECTROSCOPY; DEOXYRIBONUCLEOTIDES; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
62
Recensione:
Indirizzi per estratti:
Citazione:
F. Aslund et al., "GLUTAREDOXIN-3 FROM ESCHERICHIA-COLI - AMINO-ACID-SEQUENCE, H-1 AND N-15 NMR ASSIGNMENTS, AND STRUCTURAL-ANALYSIS", The Journal of biological chemistry, 271(12), 1996, pp. 6736-6745

Abstract

The primary and secondary structure of glutaredoxin-3 (Grx3), a glutathione-disulfide oxidoreductase from Escherichia coli, has been determined. The amino acid sequence of Grx3 consists of 82 residues and contains a redox-active motif, Cys-Pro-Tyr-Cys, typical of the glutaredoxin family. Sequence comparison reveals a homology (33% identity) to that of glutaredoxin-1 (Grx1) from E. coli as well as to other members ofthe thioredoxin superfamily. in addition to the active site cysteine residues, Grx3 contains one additional cysteine (Cys(65)) corresponding to one of the two non-active site (or structural) cysteine residues present in mammalian glutaredoxins. The sequence-specific H-1 and N-15nuclear magnetic resonance assignments of reduced Grx3 have been obtained. From a combined analysis of chemical shifts, (3)J(HN alpha) coupling constants, sequential and medium range NOEs, and amide proton exchange rates, the secondary structure of reduced Grx3 was determined and found to be very similar to that inferred from amino acid sequence comparison to homologous proteins. The consequences of the proposed structural similarity to Grx1 are that Grx3, while possessing a largely intact GSH binding cleft, would have a very different spatial distribution of charged residues, most notably surrounding the active site cysteine residues and occurring in the proposed hydrophobic protein-protein interaction area. These differences may contribute to the observed very low K-cat of Grx3 as a reductant of insulin disulfides or as a hydrogen donor for ribonucleotide reductase. Thus, despite an identical active site disulfide motif and a similar secondary structure and tertiary fold, Grx3 and Grxl display large functional differences in in vitro protein disulfide oxide-reduction reactions.

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Documento generato il 27/11/20 alle ore 12:56:13