3QLL

Crystal Structure of RipC from Yersinia pestis

Summary for 3QLL

• Entry DOI: 10.2210/pdb3qll/pdb
• Related: 3QLI 3QLK
• Descriptor: Citrate lyase (2 entities in total)
• Functional Keywords: beta barrel, citrate lyase beta subunit, lyase
• Biological source: Yersinia pestis
• Total number of polymer chains: 3
• Total formula weight: 102101.53

Authors

Torres, R.,Goulding, C.W. (deposition date: 2011-02-02, release date: 2012-01-11, Last modification date: 2024-10-16)

Primary citation

Torres, R.,Chim, N.,Sankaran, B.,Pujol, C.,Bliska, J.B.,Goulding, C.W.
Structural insights into RipC, a putative citrate lyase beta subunit from a Yersinia pestis virulence operon
Acta Crystallogr.,Sect.F, 68:2-7, 2012

PubMed Abstract: 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-γ-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 β subunit. Furthermore, the Y. pestis genome lacks genes that encode citrate lyase α and γ subunits, suggesting a unique functional role of RipC in the Y. pestis rip-mediated survival pathway. Here, the 2.45 Å resolution crystal structure of RipC revealed a homotrimer in which each monomer consists of a (β/α)(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.

PubMed: 22232161
DOI: 10.1107/S1744309111048056

Experimental method

X-RAY DIFFRACTION (2.45 Å)