3grx: Difference between revisions
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[[Image:3grx.gif|left|200px]] | [[Image:3grx.gif|left|200px]] | ||
'''NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE MIXED DISULFIDE COMPLEX, 20 STRUCTURES''' | {{Structure | ||
|PDB= 3grx |SIZE=350|CAPTION= <scene name='initialview01'>3grx</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=GTT:GLUTATHIONE'>GTT</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''NMR STRUCTURE OF ESCHERICHIA COLI GLUTAREDOXIN 3-GLUTATHIONE MIXED DISULFIDE COMPLEX, 20 STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
3GRX is a [ | 3GRX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GRX OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9973569 9973569] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thioredoxin superfamily]] | [[Category: thioredoxin superfamily]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:05:05 2008'' | ||
Revision as of 20:05, 20 March 2008
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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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