ArticleJournal of molecular biology2011
Kinetics and thermodynamics of the rate-limiting conformational change in the actomyosin V mechanochemical cycle.
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 20 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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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.
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Who cites it
20 citing papers in PubMed, 27 citations in OpenAlex.
- The order of things: phosphate release or the power stroke, which does actomyosin do first?Frontiers in physiology · 2025Review
- Switch-2 determines MgFrontiers in physiology · 2024Article
- Cell-cell interactions and fluctuations in the direction of motility promote directed migration of osteoblasts in direct current electrotaxis.Frontiers in bioengineering and biotechnology · 2022Article
- Cardiomyopathy mutations impact the actin-activated power stroke of human cardiac myosin.Biophysical journal · 2021Article
- Converter domain mutations in myosin alter structural kinetics and motor function.The Journal of biological chemistry · 2019Article
- Human Osteoblast Migration in DC Electrical Fields Depends on Store Operated CaFrontiers in bioengineering and biotechnology · 2019Article
- JED: a Java Essential Dynamics Program for comparative analysis of protein trajectories.BMC bioinformatics · 2017Article
- Direct measurements of the coordination of lever arm swing and the catalytic cycle in myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Magnesium modulates actin binding and ADP release in myosin motors.The Journal of biological chemistry · 2014Article
- Kinetics of fast changing intramolecular distance distributions obtained by combined analysis of FRET efficiency kinetics and time-resolved FRET equilibrium measurements.Biophysical journal · 2014Article
- Principal component analysis: a method for determining the essential dynamics of proteins.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Magnesium impacts myosin V motor activity by altering key conformational changes in the mechanochemical cycle.Biochemistry · 2013Article
- Global fit analysis of myosin-5b motility reveals thermodynamics of Mg2+-sensitive acto-myosin-ADP states.PloS one · 2013Article
- A subdomain interaction at the base of the lever allosterically tunes the mechanochemical mechanism of myosin 5a.PloS one · 2013Article
- Nanoscopic surfactant behavior of the porin MspA in aqueous media.Beilstein journal of nanotechnology · 2013Article
- Temperature dependent measurements reveal similarities between muscle and non-muscle myosin motility.Journal of muscle research and cell motility · 2012Article
- Mesoscopic analysis of motion and conformation of cross-bridges.Biophysical reviews · 2012Review
- Switch II mutants reveal coupling between the nucleotide- and actin-binding regions in myosin V.Biophysical journal · 2012Article
- Characterizing protein motions from structure.Journal of molecular graphics & modelling · 2011Article
- The path to visualization of walking myosin V by high-speed atomic force microscopy.Biophysical reviewsArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
We used FRET to examine the kinetics and thermodynamics of structural changes associated with ADP release in myosin V, which is thought to be a strain-sensitive step in many muscle and non-muscle myosins. We also explored essential dynamics using FIRST/FRODA starting with three different myosin V X-ray crystal structures to examine intrinsic flexibility and correlated motions. Our steady-state and time-resolved FRET analysis demonstrates a temperature-dependent reversible conformational change in the nucleotide-binding pocket (NBP). Our kinetic results demonstrate that the NBP goes from a closed to an open conformation prior to the release of ADP, while the actin-binding cleft remains closed. Interestingly, we find that the temperature dependence of the maximum actin-activated myosin V ATPase rate is similar to the pocket opening step, demonstrating that this is the rate-limiting structural transition in the ATPase cycle. Thermodynamic analysis demonstrates that the transition from the open to closed NBP conformation is unfavorable because of a decrease in entropy. The intrinsic flexibility analysis is consistent with conformational entropy playing a role in this transition as the MV.ADP structure is highly flexible compared to the MV.APO structure. Our experimental and modeling studies support the conclusion of a novel post-power-stroke actomyosin.ADP state in which the NBP and actin-binding cleft are closed. The novel state may be important for strain sensitivity as the transition from the closed to open NBP conformation may be altered by lever arm position.
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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.