3grx: Difference between revisions
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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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[[Category: Nordstrand, K.]] | [[Category: Nordstrand, K.]] | ||
[[Category: Otting, G.]] | [[Category: Otting, G.]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
[[Category: thiol-disulfide oxidoreductase]] | [[Category: thiol-disulfide oxidoreductase]] | ||
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[[Category: thioredoxin superfamily]] | [[Category: thioredoxin superfamily]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:33:40 2008'' | ||
Revision as of 05:33, 31 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE MIXED DISULFIDE COMPLEX, 20 STRUCTURES
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. 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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