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

Michael H. Godsey, Omar Davulcu, Jay C. Nix, Jack J. Skalicky, Rafael P. Brüschweiler, Michael S. Chapman

Research output: Contribution to journalArticle

4 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1658-1667
Number of pages10
JournalStructure
Volume24
Issue number10
DOIs
StatePublished - Oct 4 2016

Keywords

  • ADP
  • ambient
  • anisotropic
  • change
  • conformational
  • crystal
  • dynamics
  • induced-fit
  • protein
  • selection
  • temperature

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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    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, 24(10), 1658-1667. https://doi.org/10.1016/j.str.2016.07.013