Jacob, See Weinreb, et al., 2014 "Enhanced Amino Acid Selection in Fully-Evolved Tryptophanyl-tRNA Synthetase, Relative to its Urzyme, Requires Domain Movement Sensed by the D1 Switch, a Remote, Dynamic Packing Motif" JBC 289:4367-4376 for an especially detailed, experimentally and computationally based description of such a conformational change and its implications for substrate specificity. There is a vivid video of the most probable path taken during the catalytic cycle in the supplement, its relation to internal repacking, and its effect on the size of the tryptophan-binding pocket.
Charlie Carter On Feb 27, 2014, at 2:43 PM, Keller, Jacob wrote: Dear Crystallographers, Does anyone know of good examples of large, reversible conformational changes occurring between ligand-free and -bound states? Could also be a non-relevant molecule binding, like sulfate or something inducing dubiously -relevant changes. I already know of the calmodulin and periplasmic binding protein families, but does anyone know of others out there? All the best, Jacob Keller ******************************************* Jacob Pearson Keller, PhD Looger Lab/HHMI Janelia Farms Research Campus 19700 Helix Dr, Ashburn, VA 20147 email: kell...@janelia.hhmi.org<mailto:kell...@janelia.hhmi.org> *******************************************
