Yersinia pestis, the causative agent of the bubonic plague, and a bioterror threat, has evolved the ability to survive within activated macrophages, thereby avoiding the eukaryotic immune system. Additionally, multidrug resistance is prevalent, and new antibiotics are needed. Y. pestis encodes a novel virulence operon designated rip (required for intracellular proliferation) that encodes three proteins RipA, RipB, and RipC, of which RipA and RipB are essential. Recently, we reported a 1.9� crystal structure of RipA, a putative CoA transferase. By using enrichment factors and receiver operating characteristic plots, we evaluate the ability of docking to the crystal structure, docking to conformations sampled during a molecular dynamics (MD) simulation, and average docking scores taken over the MD conformations, to identify true positives determined during differential scanning fluorimetry assays of the National Cancer Institute's Diversity Set II. Additionally, we compare the performance of two popular docking programs, Schr�dinger's Glide and AutoDock Vina.

Optimizing lead discovery for RipA, a potential virulence factor from <i>Yersinia pestis </i>

243rd National Meeting (2012)

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Optimizing lead discovery for RipA, a potential virulence factor from Yersinia pestis