Mark A. White

TL;DR: Differences between the structures of 2C5 and 2B4 suggest that defined regions of xenobiotic metabolizing P450s may adopt a substantial range of energetically accessible conformations without perturbing the overall fold, likely to facilitate substrate access, metabolic versatility, and product egress.

TL;DR: A structural mechanism whereby ligand-induced conformational changes may coordinate catalytic activity is suggested, as well as insights into the dynamics involved in substrate access, tight inhibitor binding, and coordination of substrate and redox partner binding.

TL;DR: The results allow us to model the membrane-associated state of P450 and provide insight into how lipophilic substrates access the buried active site and identify structurally plastic regions that undergo correlated conformational changes in response to ligand binding.

TL;DR: The crystal structure of the nsP2 protease (nsP2pro) from Venezuelan equine encephalitis alphavirus determined at 2.45 A resolution is reported and shows structural similarity to S-adenosyl-L-methionine-dependent RNA methyltransferases and provides essential elements that contribute to substrate recognition and may also regulate the structure of a substrate binding cleft.