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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

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Jacob Pearson Keller, PhD
Looger Lab/HHMI Janelia Farms Research Campus
19700 Helix Dr, Ashburn, VA 20147
email: [log in to unmask]
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