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[[Image:1xw3.gif|left|200px]]<br /><applet load="1xw3" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1xw3, resolution 1.65&Aring;" />
'''Crystal Structure of Human Sulfiredoxin (Srx)'''<br />


==Overview==
==Crystal Structure of Human Sulfiredoxin (Srx)==
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.
<StructureSection load='1xw3' size='340' side='right'caption='[[1xw3]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1xw3]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XW3 FirstGlance]. <br>
1XW3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XW3 OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xw3 OCA], [https://pdbe.org/1xw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xw3 RCSB], [https://www.ebi.ac.uk/pdbsum/1xw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xw3 ProSAT]</span></td></tr>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15952770 15952770]
</table>
== Function ==
[https://www.uniprot.org/uniprot/SRXN1_HUMAN SRXN1_HUMAN] Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase.<ref>PMID:15448164</ref> <ref>PMID:15590625</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xw/1xw3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xw3 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Johnson, L C.]]
[[Category: Johnson LC]]
[[Category: Jonsson, T J.]]
[[Category: Jonsson TJ]]
[[Category: Lowther, W T.]]
[[Category: Lowther WT]]
[[Category: Murray, M S.]]
[[Category: Murray MS]]
[[Category: Poole, L B.]]
[[Category: Poole LB]]
[[Category: MPD]]
[[Category: PO4]]
[[Category: atp]]
[[Category: peroxiredoxin]]
[[Category: retroreduction]]
[[Category: sulfinic acid]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:59:13 2008''

Latest revision as of 11:53, 14 February 2024

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

Structural highlights

1xw3 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.65Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SRXN1_HUMAN Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Chang TS, Jeong W, Woo HA, Lee SM, Park S, Rhee SG. Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine. J Biol Chem. 2004 Dec 3;279(49):50994-1001. Epub 2004 Sep 24. PMID:15448164 doi:10.1074/jbc.M409482200
  2. ↑ Woo HA, Jeong W, Chang TS, Park KJ, Park SJ, Yang JS, Rhee SG. Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins. J Biol Chem. 2005 Feb 4;280(5):3125-8. Epub 2004 Dec 8. PMID:15590625 doi:10.1074/jbc.C400496200

1xw3, resolution 1.65Å

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OCA
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