ArticleProceedings of the National Academy of Sciences of the United States of America2005
Initiation of the power stroke in muscle: insights from the phosphate analog AlF4.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Single-Molecule Investigation of Load-Dependent Actomyosin Dissociation Kinetics for Cardiac and Slow Skeletal Myosin.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- High-throughput thermal denaturation of tryptophanyl-tRNA synthetase combinatorial mutants reveals high-order energetic coupling determinants of conformational stability.Structural dynamics (Melville, N.Y.) · 2023Article
- Microcalorimetry reveals multi-state thermal denaturation ofStructural dynamics (Melville, N.Y.) · 2023Article
- Actomyosin Complex.Sub-cellular biochemistry · 2022Article
- Modulation of post-powerstroke dynamics in myosin II by 2'-deoxy-ADP.Archives of biochemistry and biophysics · 2021Article
- Escapement mechanisms: Efficient free energy transduction by reciprocally-coupled gating.Proteins · 2020Article
- Single molecule mechanics resolves the earliest events in force generation by cardiac myosin.eLife · 2019Article
- Mechanistic heterogeneity in contractile properties of α-tropomyosin (TPM1) mutants associated with inherited cardiomyopathies.The Journal of biological chemistry · 2015Article
- Force-generating cross-bridges during ramp-shaped releases: evidence for a new structural state.Biophysical journal · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Motile forces in muscle are generated by the so-called "power stroke," a series of structural changes in the actomyosin cross-bridge driven by hydrolysis of ATP. The initiation of this power stroke is closely related to phosphate release after ATP cleavage and to the change of the myosin head from weak, nonstereospecific actin attachment to strong, stereospecific binding. The exact sequence of events, however, is highly controversial but crucial for the mechanism of how ATP hydrolysis drives structural changes in the head domain of myosins and related NTPases like kinesins and small G proteins. Here, we show that the phosphate analogue AlF4 can form two ADP.phosphate analog states, one with weak binding of myosin to actin and the other with strong binding of myosin to actin. Thus, change from weak to strong binding (i.e., the initiation of the power stroke) can occur before phosphate is released from the active site.
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Registered trials
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