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1xw4
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(New page: 200px<br /> <applet load="1xw4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xw4, resolution 2.00Å" /> '''Crystal Structure o...)
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Revision as of 18:05, 12 November 2007
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Crystal Structure of Human Sulfiredoxin (Srx) in Complex with ADP
Overview
Sufiredoxins (Srx) repair the inactivated forms of typical two-Cys, peroxiredoxins (Prx) implicated in hydrogen peroxide-mediated cell, signaling. The reduction of the cysteine sulfinic acid moiety within the, active site of the Prx by Srx involves novel sulfur chemistry and the use, of ATP and Mg(2+). The 1.65 A crystal structure of human Srx (hSrx), exhibits a new protein fold and a unique nucleotide binding motif, containing the Gly98-Cys99-His100-Arg101 sequence at the N-terminus of an, alpha-helix. HPLC analysis of the reaction products has confirmed that the, site of ATP cleavage is between the beta- and gamma-phosphate groups., Cys99 and the gamma-phosphate of ATP, modeled within the active site of, the 2.0 A ADP product complex structure, are adjacent to large surface, depressions containing additional conserved residues. These features and, the necessity for significant remodeling of the Prx structure suggest that, the interactions between hSrx and typical two-Cys Prxs are specific., Moreover, the concave shape of the hSrx active site surface appears to be, ideally suited to interacting with the convex surface of the toroidal Prx, decamer.
About this Structure
1XW4 is a Single protein structure of sequence from Homo sapiens with ADP as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxin., Jonsson TJ, Murray MS, Johnson LC, Poole LB, Lowther WT, Biochemistry. 2005 Jun 21;44(24):8634-42. PMID:15952770
Page seeded by OCA on Mon Nov 12 20:11:33 2007
