3qll: Difference between revisions
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==Crystal Structure of RipC from Yersinia pestis== | ==Crystal Structure of RipC from Yersinia pestis== | ||
<StructureSection load='3qll' size='340' side='right' caption='[[3qll]], [[Resolution|resolution]] 2.45Å' scene=''> | <StructureSection load='3qll' size='340' side='right'caption='[[3qll]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3qll]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3qll]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900]. 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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qli|3qli]], [[3qlk|3qlk]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qli|3qli]], [[3qlk|3qlk]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">citE2, y2383, YPO1928, YP_1670 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">citE2, y2383, YPO1928, YP_1670 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 "Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3qll" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3qll" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Phospholipase A2 homolog|Phospholipase A2 homolog]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Goulding, C W]] | [[Category: Goulding, C W]] | ||
[[Category: Torres, R]] | [[Category: Torres, R]] | ||
Revision as of 09:13, 8 June 2022
Crystal Structure of RipC from Yersinia pestisCrystal Structure of RipC from Yersinia pestis
Structural highlights
Publication Abstract from PubMedYersinia 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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