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New page: left|200px<br /> <applet load="2b6f" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b6f" /> '''Solution structure of human sulfiredoxin (S...
 
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[[Image:2b6f.gif|left|200px]]<br />
<applet load="2b6f" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2b6f" />
'''Solution structure of human sulfiredoxin (SRX)'''<br />


==Overview==
==Solution structure of human sulfiredoxin (SRX)==
The catalytic cysteine of certain members of the peroxiredoxin (Prx), family can be hyperoxidized to cysteinesulfinic acid during reduction of, peroxides. Sulfiredoxin is responsible for the ATP-dependent reduction of, cysteinesulfinic acid (SO2H) of hyperoxidized Prx. Here we report the NMR, solution structure of human sulfiredoxin (hSrx), both with and without, bound ATP, and we model the complex of ATP-bound hSrx with Prx. Binding, ATP causes only small changes in the NMR structure of hSrx, and the bound, ATP conformation is quite similar to that seen for the previously reported, X-ray structure of the ADP-hSrx complex. Although hSrx binds ATP, it does, not catalyze hydrolysis by itself and has no catalytic acid residue, typical of most ATPase and kinase family proteins. For modeling the, complex, the ATP-bound hSrx was docked to hyperoxidized Prx II using EMAP, of CHARMM. In the model complex, Asn186 of Prx II (Asp187 of Prx I) is in, contact with the hSrx-bound ATP beta- and gamma-phosphate groups. Asp187, of Prx I was mutated to alanine and asparagine, and binding and activity, of the mutants with hSrx were compared to those of the wild type. For the, D187N mutant, both binding and hydrolysis and reduction activities were, comparable to those of the wild type, whereas for D187A, binding was, unimpaired but ATP hydrolysis and reduction did not occur. The modeling, and mutagenesis analyses strongly implicate Asp187 of Prx I as the, catalytic residue responsible for ATP hydrolysis in the cysteinesulfinic, acid reduction of Prx by hSrx.
<StructureSection load='2b6f' size='340' side='right'caption='[[2b6f]]' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[2b6f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B6F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B6F FirstGlance]. <br>
2B6F 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 MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B6F OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2b6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b6f OCA], [https://pdbe.org/2b6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b6f RCSB], [https://www.ebi.ac.uk/pdbsum/2b6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b6f ProSAT]</span></td></tr>
Mutagenesis and Modeling of the Peroxiredoxin (Prx) Complex with the NMR Structure of ATP-Bound Human Sulfiredoxin Implicate Aspartate 187 of Prx I as the Catalytic Residue in ATP Hydrolysis., Lee DY, Park SJ, Jeong W, Sung HJ, Oho T, Wu X, Rhee SG, Gruschus JM, Biochemistry. 2006 Dec 26;45(51):15301-15309. Epub 2006 Dec 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17176052 17176052]
</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/b6/2b6f_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=2b6f ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ferretti, J.A.]]
[[Category: Ferretti JA]]
[[Category: Gruschus, J.M.]]
[[Category: Gruschus JM]]
[[Category: Lee, D.Y.]]
[[Category: Lee D-Y]]
[[Category: Rhee, S.G.]]
[[Category: Rhee SG]]
[[Category: ATP]]
[[Category: MG]]
[[Category: parb domain fold]]
 
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Latest revision as of 06:37, 1 May 2024

Solution structure of human sulfiredoxin (SRX)

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