1zof: Difference between revisions

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{{Seed}}
[[Image:1zof.png|left|200px]]


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==Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter Pylori==
The line below this paragraph, containing "STRUCTURE_1zof", creates the "Structure Box" on the page.
<StructureSection load='1zof' size='340' side='right'caption='[[1zof]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1zof]] is a 10 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=1ZOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZOF FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zof OCA], [https://pdbe.org/1zof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zof RCSB], [https://www.ebi.ac.uk/pdbsum/1zof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zof ProSAT]</span></td></tr>
{{STRUCTURE_1zof|  PDB=1zof  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/AHPC_HELPJ AHPC_HELPJ] Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.[UniProtKB:P0A251]
== 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/zo/1zof_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=1zof ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The AhpC protein from H. pylori, a thioredoxin (Trx)-dependent alkyl hydroperoxide-reductase, is a member of the ubiquitous 2-Cys peroxiredoxins family (2-Cys Prxs), a group of thiol-specific antioxidant enzymes. Prxs exert the protective antioxidant role in cells through their peroxidase activity, whereby hydrogen peroxide, peroxynitrite and a wide range of organic hydroperoxides (ROOH) are reduced and detoxified (ROOH + 2e(-)--&gt;ROH + H2O). In this study AhpC has been cloned and overexpressed in E. coli. After purification to homogeneity, crystals of the recombinant protein were grown. They diffract to 2.95 A resolution using synchrotron radiation. The crystal structure of AhpC has been determined using the molecular replacement method (R = 23.6%, R(free) = 25.9%). The model, similar in the overall to other members of the 2-Cys Prx family crystallized as toroide-shaped complexes, consists of a pentameric arrangement of homodimers [(alpha2)5 decamer]. The model of AhpC from H. pylori presents significant differences with respect to other members of the family: apart from some loop regions, alpha5-helix and the C-terminus is shifted, preventing the C-terminal tail of the second subunit from extending toward this region of the molecule. Oligomerization properties of AhpC have been also characterized by gel filtration chromatography.


===Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter Pylori===
Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter pylori.,Papinutto E, Windle HJ, Cendron L, Battistutta R, Kelleher D, Zanotti G Biochim Biophys Acta. 2005 Dec 1;1753(2):240-6. Epub 2005 Sep 21. PMID:16213196<ref>PMID:16213196</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_16213196}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1zof" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 16213196 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_16213196}}
__TOC__
 
</StructureSection>
==About this Structure==
1ZOF is a 10 chains structure of sequences from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOF OCA].
 
==Reference==
<ref group="xtra">PMID:16213196</ref><references group="xtra"/>
[[Category: Helicobacter pylori]]
[[Category: Helicobacter pylori]]
[[Category: Peroxiredoxin]]
[[Category: Large Structures]]
[[Category: Battistutta, R.]]
[[Category: Battistutta R]]
[[Category: Cendron, L.]]
[[Category: Cendron L]]
[[Category: Kelleher, D.]]
[[Category: Kelleher D]]
[[Category: Papinutto, E.]]
[[Category: Papinutto E]]
[[Category: Windle, H J.]]
[[Category: Windle HJ]]
[[Category: Zanotti, G.]]
[[Category: Zanotti G]]
[[Category: Decamer]]
[[Category: Toroide-shaped complex]]
 
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