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[[Image:1usp.jpg|left|200px]]
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{{STRUCTURE_1usp|  PDB=1usp  |  SCENE=  }}
'''ORGANIC HYDROPEROXIDE RESISTANCE PROTEIN FROM DEINOCOCCUS RADIODURANS'''


==Organic Hydroperoxide Resistance Protein from Deinococcus radiodurans==
<StructureSection load='1usp' size='340' side='right'caption='[[1usp]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1usp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1USP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1usp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1usp OCA], [https://pdbe.org/1usp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1usp RCSB], [https://www.ebi.ac.uk/pdbsum/1usp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1usp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9RTA8_DEIRA Q9RTA8_DEIRA]
== 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/us/1usp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1usp ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of the organic hydroperoxide resistance protein (OHRP) from Deinococcus radiodurans as determined using single crystal xray diffraction techniques is reported. Comparison of the structure with that obtained for OHRP from Pseudomonas aeruginosa reveals that the polypeptide chain of OHRPs can adopt two significantly different conformations ("in" and "out") in the region of the active site disulfide moiety. It is postulated that the closed configuration is consistent with efficient catalysis of the reduction of organic hydroperoxides, whereas the open form is required for enzyme recycling. Comparison of the structures of OHRP and that of the osmotically induced protein C (OsmC) from Mycoplasma pneumoniae shows that OHRPs and OsmCs are structurally homologous, perhaps indicating related functions for the two families of proteins.


==Overview==
The structure of the organic hydroperoxide resistance protein from Deinococcus radiodurans. Do conformational changes facilitate recycling of the redox disulfide?,Meunier-Jamin C, Kapp U, Leonard GA, McSweeney S J Biol Chem. 2004 Jun 11;279(24):25830-7. Epub 2004 Mar 30. PMID:15054099<ref>PMID:15054099</ref>
The three-dimensional structure of the organic hydroperoxide resistance protein (OHRP) from Deinococcus radiodurans as determined using single crystal xray diffraction techniques is reported. Comparison of the structure with that obtained for OHRP from Pseudomonas aeruginosa reveals that the polypeptide chain of OHRPs can adopt two significantly different conformations ("in" and "out") in the region of the active site disulfide moiety. It is postulated that the closed configuration is consistent with efficient catalysis of the reduction of organic hydroperoxides, whereas the open form is required for enzyme recycling. Comparison of the structures of OHRP and that of the osmotically induced protein C (OsmC) from Mycoplasma pneumoniae shows that OHRPs and OsmCs are structurally homologous, perhaps indicating related functions for the two families of proteins.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1USP is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USP OCA].
</div>
<div class="pdbe-citations 1usp" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The structure of the organic hydroperoxide resistance protein from Deinococcus radiodurans. Do conformational changes facilitate recycling of the redox disulfide?, Meunier-Jamin C, Kapp U, Leonard GA, McSweeney S, J Biol Chem. 2004 Jun 11;279(24):25830-7. Epub 2004 Mar 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15054099 15054099]
*[[Organic hydroperoxide resistance protein|Organic hydroperoxide resistance protein]]
[[Category: Deinococcus radiodurans]]
== References ==
[[Category: Protein complex]]
<references/>
[[Category: Kapp, U.]]
__TOC__
[[Category: Leonard, G.]]
</StructureSection>
[[Category: Mcsweeney, S.]]
[[Category: Deinococcus radiodurans R1]]
[[Category: Meunier-Jamin, C.]]
[[Category: Large Structures]]
[[Category: 2-cys peroxidase]]
[[Category: Kapp U]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:38:08 2008''
[[Category: Leonard G]]
[[Category: McSweeney S]]
[[Category: Meunier-Jamin C]]

Latest revision as of 04:57, 17 October 2024

Organic Hydroperoxide Resistance Protein from Deinococcus radiodurans

1usp, resolution 1.90Å

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