1g7o

NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2

Structural highlights 1g7o is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLRX2_ECOLI Involved in reducing some disulfide bonds in a coupled system with glutathione reductase. Does not act as hydrogen donor for ribonucleotide reductase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases.,Xia B, Vlamis-Gardikas A, Holmgren A, Wright PE, Dyson HJ J Mol Biol. 2001 Jul 20;310(4):907-18. PMID:11453697 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1g7o Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image