1xw3: Difference between revisions

Revision as of 22:15, 27 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:1xw3.png

Template:STRUCTURE 1xw3

Crystal Structure of Human Sulfiredoxin (Srx)Crystal Structure of Human Sulfiredoxin (Srx)

Template:ABSTRACT PUBMED 15952770

About this StructureAbout this Structure

1XW3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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 Sun Jul 27 22:14:37 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1xw3.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1xw3|  PDB=1xw3  |  SCENE=  }}
-'''Crystal Structure of Human Sulfiredoxin (Srx)'''
+===Crystal Structure of Human Sulfiredoxin (Srx)===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15952770}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15952770 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15952770}}
 ==About this Structure==
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 [[Category: Retroreduction]]
 [[Category: Sulfinic acid]]
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