3qll | pdb_00003qll
Crystal 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. References
| ||||||||||||||||||||||
