ArticleJournal of molecular biology2011
Nucleotide pocket thermodynamics measured by EPR reveal how energy partitioning relates myosin speed to efficiency.
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 11 papers.
What it found
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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.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Theoretical efficiency limits and speed-efficiency trade-off in myosin motors.PLoS computational biology · 2023Article
- Evolution of mechanical cooperativity among myosin II motors.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Opposing Pressures of Speed and Efficiency Guide the Evolution of Molecular Machines.Molecular biology and evolution · 2019Article
- Skeletal muscle signature of a champion sprint runner.Journal of applied physiology (Bethesda, Md. : 1985) · 2015Article
- The histone H4 tail regulates the conformation of the ATP-binding pocket in the SNF2h chromatin remodeling enzyme.Journal of molecular biology · 2014Article
- Metal switch-controlled myosin II from Dictyostelium discoideum supports closure of nucleotide pocket during ATP binding coupled to detachment from actin filaments.The Journal of biological chemistry · 2013Article
- A conformational switch in HP1 releases auto-inhibition to drive heterochromatin assembly.Nature · 2013Article
- Conformational changes at the nucleotide site in the presence of bound ADP do not set the velocity of fast Drosophila myosins.Journal of muscle research and cell motility · 2013Article
- Myosin-driven rescue of contractile reserve and energetics in mouse hearts bearing familial hypertrophic cardiomyopathy-associated mutant troponin T is mutation-specific.The Journal of physiology · 2012Article
- A novel actin binding site of myosin required for effective muscle contraction.Nature structural & molecular biology · 2012Article
- EPR spectra and molecular dynamics agree that the nucleotide pocket of myosin V is closed and that it opens on binding actin.Journal of molecular biology · 2011Article
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 2 countries.
Funding
Abstract
We have used spin-labeled ADP to investigate the dynamics of the nucleotide-binding pocket in a series of myosins, which have a range of velocities. Electron paramagnetic resonance spectroscopy reveals that the pocket is in equilibrium between open and closed conformations. In the absence of actin, the closed conformation is favored. When myosin binds actin, the open conformation becomes more favored, facilitating nucleotide release. We found that faster myosins favor a more closed pocket in the actomyosin•ADP state, with smaller values of ΔH(0) and ΔS(0), even though these myosins release ADP at a faster rate. A model involving a partitioning of free energy between work-generating steps prior to rate-limiting ADP release explains both the unexpected correlation between velocity and opening of the pocket and the observation that fast myosins are less efficient than slow myosins.
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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.