This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1fvg
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1fvg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fvg, resolution 1.6Å" /> '''CRYSTAL STRUCTURE OF ...)
Next diff →
Revision as of 13:12, 20 November 2007
|
CRYSTAL STRUCTURE OF BOVINE PEPTIDE METHIONINE SULFOXIDE REDUCTASE
Overview
Peptide methionine sulfoxide reductase (MsrA) reverses oxidative damage to, both free methionine and methionine within proteins. As such, it helps, protect the host organism against stochastic damage that can contribute to, cell death. The structure of bovine MsrA has been determined in two, different modifications, both of which provide different insights into the, biology of the protein. There are three cysteine residues located in the, vicinity of the active site. Conformational changes in a glycine-rich, C-terminal tail appear to allow all three thiols to come together and to, participate in catalysis. The structures support a unique, thiol-disulfide, exchange mechanism that relies upon an essential cysteine as a nucleophile, and additional conserved residues that interact with the oxygen atom of, the sulfoxide moiety.
About this Structure
1FVG is a Single protein structure of sequence from Bos taurus with DTT as ligand. Active as Peptide-methionine-(S)-S-oxide reductase, with EC number 1.8.4.11 Full crystallographic information is available from OCA.
Reference
Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme., Lowther WT, Brot N, Weissbach H, Matthews BW, Biochemistry. 2000 Nov 7;39(44):13307-12. PMID:11063566
Page seeded by OCA on Tue Nov 20 15:20:06 2007
