ArticleProceedings of the National Academy of Sciences of the United States of America2008
Actin-binding cleft closure in myosin II probed by site-directed spin labeling and pulsed EPR.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 52 citations in OpenAlex.
- Structural Dynamics of Protein Interactions Using Site-Directed Spin Labeling of Cysteines to Measure Distances and Rotational Dynamics with EPR Spectroscopy.Applied magnetic resonance · 2024Article
- Crowding alters F-actin secondary structure and hydration.Communications biology · 2023Article
- Article
- Modulation of post-powerstroke dynamics in myosin II by 2'-deoxy-ADP.Archives of biochemistry and biophysics · 2021Article
- Atomistic Models from Orientation and Distance Constraints Using EPR of a Bifunctional Spin Label.Biophysical journal · 2019Article
- Structural dynamics of calmodulin-ryanodine receptor interactions: electron paramagnetic resonance using stereospecific spin labels.Scientific reports · 2018Article
- The Conserved Lysine-265 Allosterically Modulates Nucleotide- and Actin-binding Site Coupling in Myosin-2.Scientific reports · 2017Article
- Oxidation increases the strength of the methionine-aromatic interaction.Nature chemical biology · 2016Article
- Macromolecular Crowding Modulates Actomyosin Kinetics.Biophysical journal · 2016Article
- Article
- Redox-sensitive residue in the actin-binding interface of myosin.Biochemical and biophysical research communications · 2014Article
- Coupling of lever arm swing and biased Brownian motion in actomyosin.PLoS computational biology · 2014Article
- Open and closed conformations of the isolated transmembrane domain of death receptor 5 support a new model of activation.Biophysical journal · 2014Article
- Electron paramagnetic resonance resolves effects of oxidative stress on muscle proteins.Exercise and sport sciences reviews · 2014Review
- Metal cation controls myosin and actomyosin kinetics.Protein science : a publication of the Protein Society · 2013Article
- Effects of ATP and actin-filament binding on the dynamics of the myosin II S1 domain.Biophysical journal · 2013Article
- Conformationally trapping the actin-binding cleft of myosin with a bifunctional spin label.The Journal of biological chemistry · 2013Article
- Article
- Global structure of a three-way junction in a phi29 packaging RNA dimer determined using site-directed spin labeling.Journal of the American Chemical Society · 2012Article
- Rigid core and flexible terminus: structure of solubilized light-harvesting chlorophyll a/b complex (LHCII) measured by EPR.The Journal of biological chemistry · 2012Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
We present a structurally dynamic model for nucleotide- and actin-induced closure of the actin-binding cleft of myosin, based on site-directed spin labeling and electron paramagnetic resonance (EPR) in Dictyostelium myosin II. The actin-binding cleft is a solvent-filled cavity that extends to the nucleotide-binding pocket and has been predicted to close upon strong actin binding. Single-cysteine labeling sites were engineered to probe mobility and accessibility within the cleft. Addition of ADP and vanadate, which traps the posthydrolysis biochemical state, influenced probe mobility and accessibility slightly, whereas actin binding caused more dramatic changes in accessibility, consistent with cleft closure. We engineered five pairs of cysteine labeling sites to straddle the cleft, each pair having one label on the upper 50-kDa domain and one on the lower 50-kDa domain. Distances between spin-labeled sites were determined from the resulting spin-spin interactions, as measured by continuous wave EPR for distances of 0.7-2 nm or pulsed EPR (double electron-electron resonance) for distances of 1.7-6 nm. Because of the high distance resolution of EPR, at least two distinct structural states of the cleft were resolved. Each of the biochemical states tested (prehydrolysis, posthydrolysis, and rigor), reflects a mixture of these structural states, indicating that the coupling between biochemical and structural states is not rigid. The resulting model is much more dynamic than previously envisioned, with both open and closed conformations of the cleft interconverting, even in the rigor actomyosin complex.
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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.