1g7o: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1g7o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G7O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G7O FirstGlance]. <br> | <table><tr><td colspan='2'>[[1g7o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G7O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G7O FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1g7o RCSB], [http://www.ebi.ac.uk/pdbsum/1g7o PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1g7o RCSB], [http://www.ebi.ac.uk/pdbsum/1g7o PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Dyson, H J | [[Category: Dyson, H J]] | ||
[[Category: Holmgren, A | [[Category: Holmgren, A]] | ||
[[Category: Vlamis-Gardikas, A | [[Category: Vlamis-Gardikas, A]] | ||
[[Category: Wright, P E | [[Category: Wright, P E]] | ||
[[Category: Xia, B | [[Category: Xia, B]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Reduced form of glutaredoxin]] | [[Category: Reduced form of glutaredoxin]] | ||
Revision as of 00:48, 23 December 2014
NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGlutaredoxin 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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