View source for 3cei


==Crystal Structure of Superoxide Dismutase from Helicobacter pylori==
<StructureSection load='3cei' size='340' side='right'caption='[[3cei]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3cei]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CEI 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3cei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cei OCA], [https://pdbe.org/3cei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cei RCSB], [https://www.ebi.ac.uk/pdbsum/3cei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cei ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SODF_HELPY SODF_HELPY] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
== 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/ce/3cei_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=3cei ConSurf].
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== Publication Abstract from PubMed ==
Superoxide dismutases (SODs) are key enzymes for fighting oxidative stress. Helicobacter pylori produces a single SOD (HpSOD) which contains iron. The structure of this antioxidant protein has been determined at 2.4 A resolution. It is a dimer of two identical subunits with one iron ion per monomer. The protein shares 53% sequence identity with the corresponding enzyme from Escherichia coli. The model is compared with those of other dimeric Fe-containing SODs. HpSOD shows significant differences in relation to other SODs, the most important being an extended C-terminal tail. This structure provides a model for closely related sequences from species such as Campylobacter, where no structures are currently known. The structure of extended carboxyl termini is discussed in light of putative functions it may serve.

The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension.,Esposito L, Seydel A, Aiello R, Sorrentino G, Cendron L, Zanotti G, Zagari A Biochim Biophys Acta. 2008 Nov;1784(11):1601-6. Epub 2008 May 6. PMID:18502213<ref>PMID:18502213</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3cei" style="background-color:#fffaf0;"></div>

==See Also==
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Helicobacter pylori]]
[[Category: Large Structures]]
[[Category: Aiello R]]
[[Category: Cendron L]]
[[Category: Esposito L]]
[[Category: Seydel A]]
[[Category: Sorrentino G]]
[[Category: Zagari A]]
[[Category: Zanotti G]]