Faculty Research
Title
The Sampling of Conformational Dynamics in Ambient-Temperature Crystal Structures of Arginine Kinase
Document Type
Article
Publication Date
2016
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 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.
DOI
10.1016/j.str.2016.07.013
CU Commons Citation
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). Faculty Research. 45.
http://commons.cu-portland.edu/msfacultyresearch/45
Comments
Publication Information.
Godsey, M. H., Davulcu, O., Nix, J. C., Skalicky, J. J., Brüschweiler, R. P., & Chapman, M. S. (2016). The sampling of conformational dynamics in ambient-temperature crystal structures of arginine kinase. Structure. doi:10.1016/j.str.2016.07.013