The critical activating conformational change common to all P-loop NTPases has traditionally been described in terms of an induced-fit model, where the presence or absence of the γ-phosphate of GTP or ATP leads to an instantaneous switch in conformation.

Our atomistic molecular simulations indicate that these enzymes harbor an intrinsic susceptibility to sample multiple conformational states regardless of the bound nucleotide. These results indicate that conformational changes in these enzymes may be best described by a population-shift mechanism rather than by the popular ligand induced-fit on/off switch model. Read More...

Tags: NTPases, kinesin, ras, rho, md, amd, evolution