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| | <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 [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> | + | <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='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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45Å</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='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='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'>[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> | | <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> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9ZC38_YERPE Q9ZC38_YERPE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Goulding, C W]] | + | [[Category: Yersinia pestis]] |
| - | [[Category: Torres, R]] | + | [[Category: Goulding CW]] |
| - | [[Category: Beta barrel]] | + | [[Category: Torres R]] |
| - | [[Category: Citrate lyase beta subunit]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
Q9ZC38_YERPE
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Torres R, Chim N, Sankaran B, Pujol C, Bliska JB, Goulding CW. Structural insights into RipC, a putative citrate lyase beta subunit from a Yersinia pestis virulence operon. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jan 1;68(Pt 1):2-7. Epub, 2011 Dec 24. PMID:22232161 doi:10.1107/S1744309111048056
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