5j99

Publication Abstract from PubMed

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.

The Sampling of Conformational Dynamics in Ambient-Temperature Crystal Structures of Arginine Kinase.,Godsey MH, Davulcu O, Nix JC, Skalicky JJ, Bruschweiler RP, Chapman MS Structure. 2016 Sep 1. pii: S0969-2126(16)30224-6. doi:, 10.1016/j.str.2016.07.013. PMID:27594681^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.