ArticleBiophysical journal2002
A classical and ab initio study of the interaction of the myosin triphosphate binding domain with ATP.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 38 citations in OpenAlex.
- Why nature really chose phosphate.Quarterly reviews of biophysics · 2013Review
- Myosin-catalyzed ATP hydrolysis elucidated by 31P NMR kinetic studies and 1H PFG-diffusion measurements.Analytical and bioanalytical chemistry · 2009Article
- New horizons of adenosinetriphosphate energetics arising from interaction with magnesium cofactor.European biophysics journal : EBJ · 2008Article
- Myosin dynamics on the millisecond time scale.Biophysical chemistry · 2007Article
- Mechanism of the myosin catalyzed hydrolysis of ATP as rationalized by molecular modeling.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Simple models for extracting mechanical work from the ATP hydrolysis cycle.Biophysical journal · 2006Article
- Protonation-induced stereoisomerism in nicotine: conformational studies using classical (AMBER) and ab initio (Car-Parrinello) molecular dynamics.Journal of computer-aided molecular design · 2005Article
- ATP hydrolysis in the betaTP and betaDP catalytic sites of F1-ATPase.Biophysical journal · 2004Article
- The conformational states of Mg.ATP in water.European biophysics journal : EBJ · 2004Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
We used classical molecular mechanics (MM) simulations and quantum mechanical (QM) structural relaxations to examine the active site of myosin when bound to ATP. Two conformations of myosin have been determined by x-ray crystallography. In one, there is no direct interaction between switch 2 and the nucleotide (open state). In the other (closed state), the universally conserved switch 2 glycine forms a hydrogen bond with a gamma-phosphate oxygen. MM simulations indicate that the two states are thermodynamically stable and allow us to investigate the extent to which the P-loop, switch 1, and switch 2 are involved in hydrolysis. We find that the open structure has a higher affinity for ATP than the closed structure, and that ATP is distorted toward a transition state by interactions with the protein. We also examine how the structure of the binding site changes with either MgATP or CaATP as the nucleotide in myosin in the open conformer. Our analyses suggest that higher CaATPase rates occur because the leaving phosphate (P(i)) group is more weakly bound and dissociation occurs faster. Finally, we validate the use of a particular formulation of a QM methodology (Car-Parrinello) to further refine the structures of the active site.
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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.