1xw3: Difference between revisions
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[[Image:1xw3.gif|left|200px]] | [[Image:1xw3.gif|left|200px]] | ||
'''Crystal Structure of Human Sulfiredoxin (Srx)''' | {{Structure | ||
|PDB= 1xw3 |SIZE=350|CAPTION= <scene name='initialview01'>1xw3</scene>, resolution 1.65Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal Structure of Human Sulfiredoxin (Srx)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1XW3 is a [ | 1XW3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XW3 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15952770 15952770] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sulfinic acid]] | [[Category: sulfinic acid]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:15:15 2008'' | ||
Revision as of 16:15, 20 March 2008
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Human Sulfiredoxin (Srx)
OverviewOverview
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 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
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