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Structural insights into RipC, a putative citrate lyase β subunit from a Yersinia pestis virulence operon

Rodrigo Torres1, Nicholas Chim, Banumathi Sankaran

  • 1Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA.

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
|January 11, 2012
PubMed

Insights

Yersinia pestis RipC protein, essential for plague virulence, has a unique structure. This research reveals RipC’s crystal structure, suggesting it binds CoA-derivatives for bacterial survival.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Yersinia pestis causes plague and is a bioterrorism concern.
  • The rip operon is crucial for Y. pestis survival in macrophages.
  • RipC's function is unique as Y. pestis lacks other citrate lyase subunits.

Purpose of the Study:

  • To elucidate the structural basis of RipC function in Y. pestis.
  • To understand RipC's role in the rip-mediated virulence pathway.

Main Methods:

  • X-ray crystallography to determine RipC structure at 2.45 Å resolution.
  • Size-exclusion chromatography to confirm the trimeric state in solution.
  • Sequence and structure comparisons with homologous proteins.

Main Results:

  • The crystal structure of RipC revealed a homotrimer.
  • Each RipC monomer exhibits a (β/α)(8) TIM-barrel fold.
  • RipC is proposed to be a CoA- or CoA-derivative binding protein.

Conclusions:

  • RipC's unique structure suggests a novel function in Y. pestis pathogenicity.
  • Understanding RipC may lead to new strategies against Y. pestis infections.
  • RipC's potential role as a CoA-binding protein warrants further investigation.

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