ArticleBiophysical journal2004
Molecular dynamics analysis of structural factors influencing back door pi release in myosin.
Article in Biophysical journal, 2004. 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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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
21 citing papers in PubMed, 54 citations in OpenAlex.
- Single-molecule tracking reveals dual front door/back door inhibition of Cel7A cellulase by its product cellobiose.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases-United in Diversity.Biomolecules · 2022Article
- Cryo-EM structure of the autoinhibited state of myosin-2.Science advances · 2021Article
- How Myosin Generates Force on Actin Filaments.Trends in biochemical sciences · 2016Review
- A gating mechanism for Pi release governs the mRNA unwinding by eIF4AI during translation initiation.Nucleic acids research · 2015Article
- Orientation of the N- and C-terminal lobes of the myosin regulatory light chain in cardiac muscle.Biophysical journal · 2015Article
- A new mechanokinetic model for muscle contraction, where force and movement are triggered by phosphate release.Journal of muscle research and cell motility · 2014Article
- Phosphate release coupled to rotary motion of F1-ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Muscle contraction mechanism based on single molecule measurements.Journal of muscle research and cell motility · 2012Article
- Myosin-V as a mechanical sensor: an elastic network study.Biophysical journal · 2012Article
- Proteomic analysis of the enterocyte brush border.American journal of physiology. Gastrointestinal and liver physiology · 2011Article
- Pi release from myosin: a simulation analysis of possible pathways.Structure (London, England : 1993) · 2010Article
- Energetics of subdomain movements and fluorescence probe solvation environment change in ATP-bound myosin.European biophysics journal : EBJ · 2008Article
- Actomyosin interaction: mechanical and energetic properties in different nucleotide binding states.International journal of molecular sciences · 2008Article
- Characterization of the pre-force-generation state in the actomyosin cross-bridge cycle.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Human deafness mutation E385D disrupts the mechanochemical coupling and subcellular targeting of myosin-1a.Biophysical journal · 2008Article
- Myosin dynamics on the millisecond time scale.Biophysical chemistry · 2007Article
- Predicting allosteric communication in myosin via a pathway of conserved residues.Journal of molecular biology · 2007Article
- High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations.The EMBO journal · 2006Article
- Control of stereoselectivity in an enzymatic reaction by backdoor access.Angewandte Chemie (International ed. in English) · 2006Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The back door has been proposed to be an exit pathway from the myosin active site for phosphate (P(i)) generated by adenosine 5'-triphosphate hydrolysis. We used molecular dynamics simulations to investigate the interaction of P(i) with the back door and the plausibility of P(i) release via this route. Molecular dynamics simulations were performed on the Dictyostelium motor domain with bound Mg.adenosine 5'-diphosphate (ADP) and P(i), modeled upon the Mg.ADP.BeF(x) and Mg.ADP.V(i) structures. Simulations revealed that the relaxation of ADP and free P(i) from their initial positions reduced the diameter of the back door via motions of switch 1 and switch 2 located in the upper and lower 50-kDa subdomains, respectively. In neither simulation could P(i) freely diffuse out the back door. Water molecules, however, could flux through the back door in the Mg.ADP.BeF(x)-based simulation but not in the Mg.ADP.V(i)-based simulation. In neither structure was water observed fluxing through the main (front door) entrance. These observations suggest that the ability of P(i) to leave via the back door is linked tightly to conformational changes between the upper and lower 50-kDa subdomains. The simulations offer structural explanations for (18)O-exchange with P(i) at the active site, and P(i) release being the rate-limiting step in the myosin adenosine 5'-triphosphatase.
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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.