View source for 3uau


==Crystal structure of the lipoprotein JlpA==
<StructureSection load='3uau' size='340' side='right'caption='[[3uau]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3uau]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni_subsp._jejuni_81-176 Campylobacter jejuni subsp. jejuni 81-176]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UAU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UAU 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]] 2.7&#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=3uau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uau OCA], [https://pdbe.org/3uau PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uau RCSB], [https://www.ebi.ac.uk/pdbsum/3uau PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uau ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H3P9U7_CAMJJ A0A0H3P9U7_CAMJJ] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Campylobacter jejuni JlpA protein is a surface-exposed lipoprotein that was discovered as an adhesin promoting interaction with host epithelium cells, an early critical step in the pathogenesis of C. jejuni disease. Increasing evidence ascertained that JlpA is antigenic, indicating a role of JlpA in immune response during the infectious process. Here, we report the crystal structure of JlpA at 2.7A resolution, revealing a catcher's mitt shaped unclosed half beta-barrel. Although the apparent architecture of JlpA is somewhat reminiscent of other bacterial lipoproteins such as LolB, the topology of JlpA is unique among the bacterial surface proteins reported to date and therefore JlpA represents a novel bacterial cell surface lipoprotein. The concave face of the structure results in an unusually large hydrophobic basin with a localized acidic pocket, suggesting a possibility that JlpA may accommodate multiple ligands. Therefore, the structure provides framework for determining the molecular function of JlpA and new strategies for the rational design of small molecule inhibitors efficiently targeting JlpA.

Crystal structure of JlpA, a surface-exposed lipoprotein adhesin of Campylobacter jejuni.,Kawai F, Paek S, Choi KJ, Prouty M, Kanipes MI, Guerry P, Yeo HJ J Struct Biol. 2012 Feb;177(2):583-8. Epub 2012 Jan 8. PMID:22245776<ref>PMID:22245776</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3uau" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Campylobacter jejuni subsp. jejuni 81-176]]
[[Category: Large Structures]]
[[Category: Kawai F]]
[[Category: Yeo HJ]]