Nuclear magnetic resonance studies of recombinant Escherichia coli glutaredoxin: Sequence‐specific assignments and secondary structure determination of the oxidized form

Patrick SODANO, Kandala V.R. CHARY, Olof BJÖRNBERG, Arne HOLMGREN, Betsy KREN, James A. FUCHS, Kurt WÜTHRICH

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Escherichia coli glutaredoxin (85 amino acid residues, Mr= 9100), the glutathione‐dependent hydrogen donor for ribonucleotide reductase, was purified from an inducible λpl expression system both with a natural isotope content and with uniform 15N labelling. This material was used for obtaining sequence‐specific 1H magnetic resonance assignments and the identification of regular secondary structures in the oxidized form of the protein, which contains the redox‐active disulfide . Oxidized glutaredoxin contains a four‐stranded β‐sheet, with the peripheral strand 32–37 arranged parallel to the strand 2–7, which further combines with the two additional strands 61–64 and 67–69 in an antiparallel fashion. The protein further contains three helices extending approximately from residues 13–28, 45–54 and 72–84.

Original languageEnglish (US)
Pages (from-to)369-377
Number of pages9
JournalEuropean Journal of Biochemistry
Volume200
Issue number2
DOIs
StatePublished - Sep 1991

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