ArticleStructure (London, England : 1993)2009
Intrinsic domain and loop dynamics commensurate with catalytic turnover in an induced-fit enzyme.
Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Article
- Structure of McsB, a protein kinase for regulated arginine phosphorylation.Nature chemical biology · 2019Article
- 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
- The Sampling of Conformational Dynamics in Ambient-Temperature Crystal Structures of Arginine Kinase.Structure (London, England : 1993) · 2016Article
- Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell.Chemical reviews · 2016Review
- Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data.Angewandte Chemie (International ed. in English) · 2016Article
- HdeB chaperone activity is coupled to its intrinsic dynamic properties.Scientific reports · 2015Article
- 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
- Enzyme dynamics from NMR spectroscopy.Accounts of chemical research · 2015Review
- Identifying sequential substrate binding at the single-molecule level by enzyme mechanical stabilization.ACS nano · 2015Article
- Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form.Biomolecular NMR assignments · 2014Article
- Crystal structures of arginine kinase in complex with ADP, nitrate, and various phosphagen analogs.Biochemical and biophysical research communications · 2012Article
- Rate-limiting domain and loop motions in arginine kinase.Biochemistry · 2011Article
- The structure of lombricine kinase: implications for phosphagen kinase conformational changes.The Journal of biological chemistry · 2011Article
- Arginine kinase: joint crystallographic and NMR RDC analyses link substrate-associated motions to intrinsic flexibility.Journal of molecular biology · 2011Article
- Enzyme dynamics point to stepwise conformational selection in catalysis.Current opinion in chemical biology · 2010Review
- Direct evidence of conformational heterogeneity in human pancreatic glucokinase from high-resolution nuclear magnetic resonance.Biochemistry · 2010Article
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4 authors.
Funding
Abstract
Arginine kinase catalyzes reversible phosphoryl transfer between ATP and arginine, buffering cellular ATP concentrations. Structures of substrate-free and -bound enzyme have highlighted a range of conformational changes thought to occur during the catalytic cycle. Here, NMR is used to characterize the intrinsic backbone dynamics over multiple timescales. Relaxation dispersion indicates rigid-body motion of the N-terminal domain and flexible dynamics in the I182-G209 loop, both at millisecond rates commensurate with k(cat), implying that either might be rate limiting upon catalysis. Lipari-Szabo analysis indicates backbone flexibility on the nanosecond timescale in the V308-V322 loop, while the rest of the enzyme is more rigid in this timescale. Thus, intrinsic dynamics are most prominent in regions that have been independently implicated in conformational changes. Substrate-free enzyme may sample an ensemble of different conformations, of which a subset is selected upon substrate binding, with critical active site residues appropriately configured for binding and catalysis.
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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.