1xw3

From Proteopedia

(Difference between revisions)

Revision as of 07:27, 18 April 2018

Crystal Structure of Human Sulfiredoxin (Srx)

Structural highlights

1xw3 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1xw4
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.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ 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
↑ Jonsson TJ, Murray MS, Johnson LC, Poole LB, Lowther WT. Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxin. Biochemistry. 2005 Jun 21;44(24):8634-42. PMID:15952770 doi:10.1021/bi050131i

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xw3"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Human Sulfiredoxin (Srx)==
 <StructureSection load='1xw3' size='340' side='right' caption='[[1xw3]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xw4|1xw4]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xw3 OCA], [http://pdbe.org/1xw3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xw3 RCSB], [http://www.ebi.ac.uk/pdbsum/1xw3 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xw3 OCA], [http://pdbe.org/1xw3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xw3 RCSB], [http://www.ebi.ac.uk/pdbsum/1xw3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xw3 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xw/1xw3_consurf.spt"</scriptWhenChecked>
+    <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>
@@ Line 38: / Line 39: @@
 [[Category: Murray, M S]]
 [[Category: Poole, L B]]
+[[Category: Atp]]
 [[Category: Oxidoreductase]]
 [[Category: Peroxiredoxin]]
 [[Category: Retroreduction]]
 [[Category: Sulfinic acid]]

1xw3

From Proteopedia

Revision as of 07:27, 18 April 2018

Crystal Structure of Human Sulfiredoxin (Srx)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox