View source for 3lwg


==Crystal structure of HP0420-homologue C46A from helicobacter felis==
<StructureSection load='3lwg' size='340' side='right'caption='[[3lwg]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3lwg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_felis Helicobacter felis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LWG 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]] 1.8&#8491;</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=3lwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lwg OCA], [https://pdbe.org/3lwg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lwg RCSB], [https://www.ebi.ac.uk/pdbsum/3lwg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lwg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D5MNX9_HELFE D5MNX9_HELFE] 
== 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/lw/3lwg_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=3lwg ConSurf].
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== Publication Abstract from PubMed ==
Helicobacter pylori infect more than half of the world's population and are considered a cause of peptic ulcer disease and gastric cancer. Recently, hypothetical gene HP0421 was identified in H. pylori as a cholesterol alpha-glucosyltransferase, which is required to synthesize cholesteryl glucosides, essential cell wall components of the bacteria. In the same gene-cluster, HP0420 was co-identified, whose function remains unknown. Here we report the crystal structure of HP0420-homolog of H. felis (HF0420) to gain insight into the function of HP0420. The crystal structure, combined with size-exclusion chromatography, reveals that HF0420 adopts a homodimeric hot-dog fold. The crystal structure suggests that HF0420 has enzymatic activity that involves a conserved histidine residue at the end of the central alpha-helix. Subsequent biochemical studies provide clues to the function of HP0420 and HF0420.

Crystal structure and functional insight of HP0420-homolog from Helicobacter felis.,Piao S, Jin XL, Yun BY, Kim N, Cho HS, Fukuda M, Lee H, Ha NC Biochem Biophys Res Commun. 2010 Apr 16;394(4):940-6. Epub 2010 Mar 17. PMID:20302842<ref>PMID:20302842</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 3lwg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Helicobacter felis]]
[[Category: Large Structures]]
[[Category: Ha N-C]]
[[Category: Piao S]]