ArticleProceedings of the National Academy of Sciences of the United States of America1997
The structure of the acto-myosin subfragment 1 complex: results of searches using data from electron microscopy and x-ray crystallography.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. 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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30 citing papers in PubMed, 71 citations in OpenAlex.
- Amplitude of the actomyosin power stroke depends strongly on the isoform of the myosin essential light chain.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Conventions and workflows for using Situs.Acta crystallographica. Section D, Biological crystallography · 2012Article
- Matching structural densities from different biophysical origins with gain and bias.Journal of structural biology · 2011Article
- FRET characterisation for cross-bridge dynamics in single-skinned rigor muscle fibres.European biophysics journal : EBJ · 2011Article
- Unidirectional Brownian motion observed in an in silico single molecule experiment of an actomyosin motor.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Article
- Molecular dynamics flexible fitting: a practical guide to combine cryo-electron microscopy and X-ray crystallography.Methods (San Diego, Calif.) · 2009Article
- The myosin C-loop is an allosteric actin contact sensor in actomyosin.Biochemistry · 2009Article
- Close proximity of myosin loop 3 to troponin determined by triangulation of resonance energy transfer distance measurements.Biochemistry · 2009Article
- Close packing of Listeria monocytogenes ActA, a natively unfolded protein, enhances F-actin assembly without dimerization.The Journal of biological chemistry · 2008Article
- Diversity of structural behavior in vertebrate conventional myosins complexed with actin.Journal of molecular biology · 2007Article
- Structural changes of cross-bridges on transition from isometric to shortening state in frog skeletal muscle.Biophysical journal · 2006Article
- Structural changes of actin-bound myosin heads after a quick length change in frog skeletal muscle.Biophysical journal · 2005Article
- Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- The prepower stroke conformation of myosin V.The Journal of cell biology · 2002Article
- Addition of missing loops and domains to protein models by x-ray solution scattering.Biophysical journal · 2002Article
- Coordination of the two heads of myosin during muscle contraction.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Molecular dynamics simulation of site-directed spin labeling: experimental validation in muscle fibers.Biophysical journal · 2002Article
- Direct modeling of x-ray diffraction pattern from skeletal muscle in rigor.Biophysical journal · 2002Article
- A model of cross-bridge attachment to actin in the A*M*ATP state based on x-ray diffraction from permeabilized rabbit psoas muscle.Biophysical journal · 2002Article
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
Abstract
Surmises of how myosin subfragment 1 (S1) interacts with actin filaments in muscle contraction rest upon knowing the relative arrangement of the two proteins. Although there exist crystallographic structures for both S1 and actin, as well as electron microscopy data for the acto-S1 complex (AS1), modeling of this arrangement has so far only been done "by eye." Here we report fitted AS1 structures obtained using a quantitative method that is both more objective and makes more complete use of the data. Using undistorted crystallographic results, the best-fit AS1 structure shows significant differences from that obtained by visual fitting. The best fit is produced using the F-actin model of Holmes et al. [Holmes, K. C., Popp, D., Gebhard, W. & Kabsch, W. (1990) Nature (London) 347, 44-49]. S1 residues at the AS1 interface are now found at a higher radius as well as being translated axially and rotated azimuthally. Fits using S1 plus loops missing from the crystal structure were achieved using a homology search method to predict loop structures. These improved fits favor an arrangement in which the loop at the 50- to 20-kDa domain junction of S1 is located near the N terminus of actin. Rigid-body movements of the lower 50-kDa domain, which further improve the fit, produce closure of the large 50-kDa domain cleft and bring conserved residues in the lower 50-kDa domain into an apparently appropriate orientation for close interaction with actin. This finding supports the idea that binding of ATP to AS1 at the end of the ATPase cycle disrupts the actin binding site by changing the conformation of the 50-kDa cleft of S1.
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