ArticleJournal of molecular biology2011
Arginine kinase: joint crystallographic and NMR RDC analyses link substrate-associated motions to intrinsic flexibility.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed.
- NMR methods for investigating functionally relevant biomolecular dynamics.Magnetic resonance letters · 2025Review
- A comprehensive review of arginine kinase proteins: What we need to know?Biochemistry and biophysics reports · 2024Review
- Crystal Structure of H227A Mutant of Arginine Kinase inMolecules (Basel, Switzerland) · 2022Article
- Molecular insights on CALX-CBD12 interdomain dynamics from MD simulations, RDCs, and SAXS.Biophysical journal · 2021Article
- Insight into Structural Aspects of Histidine 284 ofMolecules and cells · 2020Article
- Natural Products Containing 'Rare' Organophosphorus Functional Groups.Molecules (Basel, Switzerland) · 2019Review
- Elevated μs-ms timescale backbone dynamics in the transition state analog form of arginine kinase.Journal of structural biology · 2017Article
- The Michaelis Complex of Arginine Kinase Samples the Transition State at a Frequency That Matches the Catalytic Rate.Journal of the American Chemical Society · 2017Article
- Absolute Minimal Sampling in High-Dimensional NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2016Article
- The Sampling of Conformational Dynamics in Ambient-Temperature Crystal Structures of Arginine Kinase.Structure (London, England : 1993) · 2016Article
- Parsimony in Protein Conformational Change.Structure (London, England : 1993) · 2015Article
- The substrate-free and -bound crystal structures of the duplicated taurocyamine kinase from the human parasite Schistosoma mansoni.The Journal of biological chemistry · 2015Article
- Promiscuous and specific recognition among ephrins and Eph receptors.Biochimica et biophysica acta · 2014Article
- Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form.Biomolecular NMR assignments · 2014Article
- Stabilization of the dimeric birch pollen allergen Bet v 1 impacts its immunological properties.The Journal of biological chemistry · 2014Article
- Crystal structures of arginine kinase in complex with ADP, nitrate, and various phosphagen analogs.Biochemical and biophysical research communications · 2012Article
- Crystallization and X-ray diffraction studies of arginine kinase from the white Pacific shrimp Litopenaeus vannamei.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Substrate-specific reorganization of the conformational ensemble of CSK implicates novel modes of kinase function.PLoS computational biology · 2012Article
- Expanding the proteome: disordered and alternatively folded proteins.Quarterly reviews of biophysics · 2011Article
- Rate-limiting domain and loop motions in arginine kinase.Biochemistry · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
The phosphagen kinase family, including creatine and arginine kinases (AKs), catalyzes the reversible transfer of a "high-energy" phosphate between ATP and a phosphoguanidino substrate. They have become a model for the study of both substrate-induced conformational change and intrinsic protein dynamics. Prior crystallographic studies indicated large substrate-induced domain rotations, but differences among a recent set of AK structures were interpreted as a plastic deformation. Here, the structure of Limulus substrate-free AK is refined against high-resolution crystallographic data and compared quantitatively with NMR chemical shifts and residual dipolar couplings (RDCs). This demonstrates the feasibility of this type of RDC analysis of proteins that are large by NMR standards (42 kDa) and illuminates the solution structure, free from crystal-packing constraints. Detailed comparison of the 1.7 Å resolution substrate-free crystal structure against the 1.7 Å transition-state analog complex shows large substrate-induced domain motions that can be broken down into movements of smaller quasi-rigid bodies. The solution-state structure of substrate-free AK is most consistent with an equilibrium of substrate-free and substrate-bound structures, with the substrate-free form dominating, but with varying displacements of the quasi-rigid groups. Rigid-group rotations evident from the crystal structures are about axes previously associated with intrinsic millisecond dynamics using NMR relaxation dispersion. Thus, "substrate-induced" motions are along modes that are intrinsically flexible in the substrate-free enzyme and likely involve some degree of conformational selection.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.