The Sampling of Conformational Dynamics in Ambient-Temperature Crystal Structures of Arginine Kinase
Arginine kinase provides a model for functional dynamics, studied through crystallography, enzymology, and nuclear magnetic resonance. Structures are now solved, at ambient temperature, for the transition state analog (TSA) complex. Analysis of quasi-rigid sub-domain displacements show that differences between the two TSA structures average about 5% of changes between substrate-free and TSA forms, and they are nearly co-linear. Small backbone hinge rotations map to sites that also flex on substrate binding. Anisotropic atomic displacement parameters (ADPs) are refined using rigid-body TLS constraints. Consistency between crystal forms shows that they reflect intrinsic molecular properties more than crystal lattice effects. In many regions, the favored directions of thermal/static displacement are appreciably correlated with movements on substrate binding. Correlation between ADPs and larger substrate-associated movements implies that the latter approximately follow paths of low-energy intrinsic motions.
Godsey, Michael H.; Davulcu, Omar; Nix, Jay C.; Skalicky, Jack J.; Brüschweiler, Rafael P.; and Chapman, Michael S., "The Sampling of Conformational Dynamics in Ambient-Temperature Crystal Structures of Arginine Kinase" (2016). CUP Faculty Research. 136.
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