ArticleStructure (London, England : 1993)2016
The Sampling of Conformational Dynamics in Ambient-Temperature Crystal Structures of Arginine Kinase.
Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Structural Insights into Arginine Kinase and Phosphagen Kinase Homologs: Mechanisms of Catalysis, Regulation, and Evolution.Biology · 2025Review
- A comprehensive review of arginine kinase proteins: What we need to know?Biochemistry and biophysics reports · 2024Review
- Changes in Active Site Loop Conformation Relate to the Transition toward a Novel Enzymatic Activity.JACS Au · 2024Article
- Crystal Structure of H227A Mutant of Arginine Kinase inMolecules (Basel, Switzerland) · 2022Article
- Structural and dynamical description of the enzymatic reaction of a phosphohexomutase.Structural dynamics (Melville, N.Y.) · 2019Article
- Elevated μs-ms timescale backbone dynamics in the transition state analog form of arginine kinase.Journal of structural biology · 2017Article
Corrections and comments
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Authors and funding
6 authors.
Funding
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.
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Registered trials
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