1g7o: Difference between revisions

Revision as of 04:50, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1g7o.png

Template:STRUCTURE 1g7o

NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2

Template:ABSTRACT PUBMED 11453697

About this StructureAbout this Structure

1G7O is a Single protein structure of sequence from Escherichia coli. Full experimental 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

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-'''NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2'''
+===NMR SOLUTION STRUCTURE OF REDUCED E. COLI GLUTAREDOXIN 2===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11453697}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11453697}}
 ==About this Structure==
-G7O 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=1G7O OCA].
+G7O is a [[Single protein]] structure of 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].
 ==Reference==
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 [[Category: Nmr]]
 [[Category: Reduced form of glutaredoxin]]
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