3grx

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3grx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3grx OCA], [http://www.ebi.ac.uk/pdbsum/3grx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3grx RCSB]</span>
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'''NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE MIXED DISULFIDE COMPLEX, 20 STRUCTURES'''
'''NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE MIXED DISULFIDE COMPLEX, 20 STRUCTURES'''
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[[Category: Nordstrand, K.]]
[[Category: Nordstrand, K.]]
[[Category: Otting, G.]]
[[Category: Otting, G.]]
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[[Category: electron transport]]
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[[Category: Electron transport]]
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[[Category: thiol-disulfide oxidoreductase]]
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[[Category: Thiol-disulfide oxidoreductase]]
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[[Category: thioltransferase]]
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[[Category: Thioltransferase]]
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[[Category: thioredoxin superfamily]]
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[[Category: Thioredoxin superfamily]]
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Revision as of 19:03, 4 May 2008

Template:STRUCTURE 3grx

NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE MIXED DISULFIDE COMPLEX, 20 STRUCTURES


Overview

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 Structure

3GRX is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 22:03:05 2008

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