1G7O

NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2

Summary for 1G7O

• Entry DOI: 10.2210/pdb1g7o/pdb
• Descriptor: GLUTAREDOXIN 2 (1 entity in total)
• Functional Keywords: reduced form of glutaredoxin, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 24383.23

Authors

Xia, B.,Vlamis-Gardikas, A.,Holmgren, A.,Wright, P.E.,Dyson, H.J. (deposition date: 2000-11-10, release date: 2001-07-20, Last modification date: 2024-05-22)

Primary citation

Xia, B.,Vlamis-Gardikas, A.,Holmgren, A.,Wright, P.E.,Dyson, H.J.
Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases.
J.Mol.Biol., 310:907-918, 2001

PubMed Abstract: Glutaredoxin 2 (Grx2) from Escherichia coli is distinguished from other glutaredoxins by its larger size, low overall sequence identity and lack of electron donor activity with ribonucleotide reductase. However, catalysis of glutathione (GSH)-dependent general disulfide reduction by Grx2 is extremely efficient. The high-resolution solution structure of E. coli Grx2 shows a two-domain protein, with residues 1 to 72 forming a classical "thioredoxin-fold" glutaredoxin domain, connected by an 11 residue linker to the highly helical C-terminal domain, residues 84 to 215. The active site, Cys9-Pro10-Tyr11-Cys12, is buried in the interface between the two domains, but Cys9 is solvent-accessible, consistent with its role in catalysis. The structures reveal the hither to unknown fact that Grx2 is structurally similar to glutathione-S-transferases (GST), although there is no obvious sequence homology. The similarity of these structures gives important insights into the functional significance of a new class of mammalian GST-like proteins, the single-cysteine omega class, which have glutaredoxin oxidoreductase activity rather than GSH-S-transferase conjugating activity. E. coli Grx 2 is structurally and functionally a member of this new expanding family of large glutaredoxins. The primary function of Grx2 as a GST-like glutaredoxin is to catalyze reversible glutathionylation of proteins with GSH in cellular redox regulation including stress responses.

PubMed: 11453697
DOI: 10.1006/jmbi.2001.4721

Experimental method

SOLUTION NMR