3grx
NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE MIXED DISULFIDE COMPLEX, 20 STRUCTURES
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OverviewOverview
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 a well-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 the reduction 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 a reductant 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.
About this StructureAbout this Structure
3GRX is a Single protein structure of sequence from Escherichia coli with GTT as ligand. Full crystallographic information is available from OCA.
ReferenceReference
NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism., Nordstrand K, slund F, Holmgren A, Otting G, Berndt KD, J Mol Biol. 1999 Feb 19;286(2):541-52. PMID:9973569
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