View source for 3qll


==Crystal Structure of RipC from Yersinia pestis==
<StructureSection load='3qll' size='340' side='right'caption='[[3qll]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qll]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QLL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QLL 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]] 2.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=3qll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qll OCA], [https://pdbe.org/3qll PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qll RCSB], [https://www.ebi.ac.uk/pdbsum/3qll PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qll ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9ZC38_YERPE Q9ZC38_YERPE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Yersinia pestis remains a threat, with outbreaks of plague occurring in rural areas and its emergence as a weapon of bioterrorism; thus, an improved understanding of its various pathogenicity pathways is warranted. The rip (required for intracellular proliferation) virulence operon is required for Y. pestis survival in interferon-gamma-treated macrophages and has been implicated in lowering macrophage-produced nitric oxide levels. RipC, one of three gene products from the rip operon, is annotated as a citrate lyase beta subunit. Furthermore, the Y. pestis genome lacks genes that encode citrate lyase alpha and gamma subunits, suggesting a unique functional role of RipC in the Y. pestis rip-mediated survival pathway. Here, the 2.45 A resolution crystal structure of RipC revealed a homotrimer in which each monomer consists of a (beta/alpha)(8) TIM-barrel fold. Furthermore, the trimeric state was confirmed in solution by size-exclusion chromatography. Through sequence and structure comparisons with homologous proteins, it is proposed that RipC is a putative CoA- or CoA-derivative binding protein.

Structural insights into RipC, a putative citrate lyase beta subunit from a Yersinia pestis virulence operon.,Torres R, Chim N, Sankaran B, Pujol C, Bliska JB, Goulding CW Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jan 1;68(Pt 1):2-7. Epub, 2011 Dec 24. PMID:22232161<ref>PMID:22232161</ref>

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

==See Also==
*[[Phospholipase A2 homolog|Phospholipase A2 homolog]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Yersinia pestis]]
[[Category: Goulding CW]]
[[Category: Torres R]]