1g7o: Difference between revisions
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g7o OCA], [http://www.ebi.ac.uk/pdbsum/1g7o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g7o RCSB]</span> | |||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: reduced form of glutaredoxin]] | [[Category: reduced form of glutaredoxin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:38:21 2008'' | ||
Revision as of 20:38, 30 March 2008
| |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2
OverviewOverview
Glutaredoxin 2 (Grx2) from Escherichia coli is distinguished from other glutaredoxins by its larger size, low overall sequence identity and lack of electron donor activity with ribonucleotide reductase. However, catalysis of glutathione (GSH)-dependent general disulfide reduction by Grx2 is extremely efficient. The high-resolution solution structure of E. coli Grx2 shows a two-domain protein, with residues 1 to 72 forming a classical "thioredoxin-fold" glutaredoxin domain, connected by an 11 residue linker to the highly helical C-terminal domain, residues 84 to 215. The active site, Cys9-Pro10-Tyr11-Cys12, is buried in the interface between the two domains, but Cys9 is solvent-accessible, consistent with its role in catalysis. The structures reveal the hither to unknown fact that Grx2 is structurally similar to glutathione-S-transferases (GST), although there is no obvious sequence homology. The similarity of these structures gives important insights into the functional significance of a new class of mammalian GST-like proteins, the single-cysteine omega class, which have glutaredoxin oxidoreductase activity rather than GSH-S-transferase conjugating activity. E. coli Grx 2 is structurally and functionally a member of this new expanding family of large glutaredoxins. The primary function of Grx2 as a GST-like glutaredoxin is to catalyze reversible glutathionylation of proteins with GSH in cellular redox regulation including stress responses.
About this StructureAbout this Structure
1G7O is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases., Xia B, Vlamis-Gardikas A, Holmgren A, Wright PE, Dyson HJ, J Mol Biol. 2001 Jul 20;310(4):907-18. PMID:11453697
Page seeded by OCA on Sun Mar 30 20:38:21 2008