ArticleProceedings of the National Academy of Sciences of the United States of America2014
Catalytic strategy used by the myosin motor to hydrolyze ATP.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 65 citations in OpenAlex.
- Mutation-induced free-energy remodeling of recovery stroke and ATP hydrolysis in human cardiac β-myosin.Biophysical journal · 2026Article
- Structural Biology of Actin: Interplay Between Molecular Assembly, Conformational Polymorphism and ATPase.Sub-cellular biochemistry · 2026Review
- Mechanism, Efficacy, and Safety of Natural Antibiotics.Antibiotics (Basel, Switzerland) · 2025Review
- Dynamics of the Pre-Powerstroke Myosin Lever Arm and the Effects of Omecamtiv Mecarbil.International journal of molecular sciences · 2024Article
- Myosin-Catalyzed ATP Hydrolysis in the Presence of Disease-Causing Mutations: Mavacamten as a Way to Repair Mechanism.The journal of physical chemistry. B · 2024Article
- A weak coupling mechanism for the early steps of the recovery stroke of myosin VI: A free energy simulation and string method analysis.PLoS computational biology · 2024Article
- Insights into the Mechanism of the Cardiac Drug Omecamtiv Mecarbil─A Computational Study.The journal of physical chemistry. B · 2022Article
- Structures and mechanisms of actin ATP hydrolysis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- COVID-19: the CaMKII-like system of S protein drives membrane fusion and induces syncytial multinucleated giant cells.Immunologic research · 2021Article
- Investigation of the Recovery Stroke and ATP Hydrolysis and Changes Caused Due to the Cardiomyopathic Point Mutations in Human Cardiac β Myosin.The journal of physical chemistry. B · 2021Article
- miR-29c&b2 encourage extramedullary infiltration resulting in the poor prognosis of acute myeloid leukemia.Oncogene · 2021Article
- Mechanochemical Function of Myosin II: Investigation into the Recovery Stroke and ATP Hydrolysis.The journal of physical chemistry. B · 2020Article
- Inorganic Polyphosphates As Storage for and Generator of Metabolic Energy in the Extracellular Matrix.Chemical reviews · 2019Review
- Mapping Free Energy Pathways for ATP Hydrolysis in theMolecules (Basel, Switzerland) · 2018Article
- Thiacalix[4]arenes Remove the Inhibitory Effects of Zn Cations on the Myosin ATPase Activity.Nanoscale research letters · 2018Article
- Analysis of Phosphoryl-Transfer Enzymes with QM/MM Free Energy Simulations.Methods in enzymology · 2018Article
- Mechanism by which water and protein electrostatic interactions control proton transfer at the active site of channelrhodopsin.PloS one · 2018Article
- Metal Fluorides: Tools for Structural and Computational Analysis of Phosphoryl Transfer Enzymes.Topics in current chemistry (Cham) · 2017Review
- Regulation and Plasticity of Catalysis in Enzymes: Insights from Analysis of Mechanochemical Coupling in Myosin.Biochemistry · 2017Article
- The GTPase hGBP1 converts GTP to GMP in two stepsChemical science · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myosin is a molecular motor responsible for biological motions such as muscle contraction and intracellular cargo transport, for which it hydrolyzes adenosine 5'-triphosphate (ATP). Early steps of the mechanism by which myosin catalyzes ATP hydrolysis have been investigated, but still missing are the structure of the final ADP·inorganic phosphate (Pi) product and the complete pathway leading to it. Here, a comprehensive description of the catalytic strategy of myosin is formulated, based on combined quantum-classical molecular mechanics calculations. A full exploration of catalytic pathways was performed and a final product structure was found that is consistent with all experiments. Molecular movies of the relevant pathways show the different reorganizations of the H-bond network that lead to the final product, whose γ-phosphate is not in the previously reported HPγO4(2-) state, but in the H2PγO4(-) state. The simulations reveal that the catalytic strategy of myosin employs a three-pronged tactic: (i) Stabilization of the γ-phosphate of ATP in a dissociated metaphosphate (PγO3(-)) state. (ii) Polarization of the attacking water molecule, to abstract a proton from that water. (iii) Formation of multiple proton wires in the active site, for efficient transfer of the abstracted proton to various product precursors. The specific role played in this strategy by each of the three loops enclosing ATP is identified unambiguously. It explains how the precise timing of the ATPase activation during the force generating cycle is achieved in myosin. The catalytic strategy described here for myosin is likely to be very similar in most nucleotide hydrolyzing enzymes.
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