The Sampling of Conformational Dynamics in Ambient-Temperature Crystal Structures of Arginine Kinase.

ABSTRACT: 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 displacem

SUBMITTER: Godsey MH 

PROVIDER: S-EPMC5052116 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature