Active site details of bacterial VapC toxins revealed

Crystal structure of the dimeric, isolated VapC toxin from Shigella flexneri.

Crystal structure of the dimeric, isolated VapC toxin from Shigella flexneri (Xu et al., Proteins, 2016).

Today, our lab published a comprehensive, structural analysis of the active site configuration observed in the Shigella flexneri VapC toxin RNase. By comparison to bacterial RNase H, we show that there are in up to five residues that are conserved in the active site, and not three as has previously been believed. We are also able to model substrate in the active site by analogy to RNase H, providing a first glimpse at what the molecular mechanism of catalysis might be for the PIN domain bacterial RNases.

For more information, have a look at the paper in Proteins.

Xu K., Dedic E., and Brodersen D. E. (2016) “Structural analysis on the active site architecture of the VapC toxin from Shigella flexneri”, Proteins, 84(7):892-899.