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1fov
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(New page: 200px<br /><applet load="1fov" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fov" /> '''GLUTAREDOXIN 3 FROM ESCHERICHIA COLI IN THE ...)
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Revision as of 12:59, 20 November 2007
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GLUTAREDOXIN 3 FROM ESCHERICHIA COLI IN THE FULLY OXIDIZED FORM
Overview
A high precision NMR structure of oxidized glutaredoxin 3 [C65Y] from, Escherichia coli has been determined. The conformation of the active site, including the disulphide bridge is highly similar to those in, glutaredoxins from pig liver and T4 phage. A comparison with the, previously determined structure of glutaredoxin 3 [C14S, C65Y] in a, complex with glutathione reveals conformational changes between the free, and substrate-bound form which includes the sidechain of the conserved, active site tyrosine residue. In the oxidized form this tyrosine is, solvent exposed, while it adopts a less exposed conformation, stabilized, by hydrogen bonds, in the mixed disulfide with glutathione. The structures, further suggest that the formation of a covalent linkage between, glutathione and glutaredoxin 3 is necessary in order to induce these, structural changes upon binding of the glutathione peptide. This could, explain the observed low affinity of glutaredoxins for S-blocked, glutathione analogues, in spite of the fact that glutaredoxins are highly, specific reductants of glutathione mixed disulfides.
About this Structure
1FOV is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
NMR structure of oxidized glutaredoxin 3 from Escherichia coli., Nordstrand K, Sandstrom A, Aslund F, Holmgren A, Otting G, Berndt KD, J Mol Biol. 2000 Oct 27;303(3):423-32. PMID:11031118
Page seeded by OCA on Tue Nov 20 15:06:13 2007
