3GRX
NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE MIXED DISULFIDE COMPLEX, 20 STRUCTURES
Summary for 3GRX
| Entry DOI | 10.2210/pdb3grx/pdb |
| NMR Information | BMRB: 4225 |
| Descriptor | GLUTAREDOXIN 3, GLUTATHIONE (2 entities in total) |
| Functional Keywords | electron transport, thiol-disulfide oxidoreductase, thioltransferase, thioredoxin superfamily |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 9370.60 |
| Authors | Nordstrand, K.,Aslund, F.,Holmgren, A.,Otting, G.,Berndt, K.D. (deposition date: 1998-08-17, release date: 1999-03-30, Last modification date: 2025-03-26) |
| Primary citation | Nordstrand, K.,slund, F.,Holmgren, A.,Otting, G.,Berndt, K.D. NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism. J.Mol.Biol., 286:541-552, 1999 Cited by PubMed Abstract: 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. PubMed: 9973569DOI: 10.1006/jmbi.1998.2444 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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