ArticleProceedings of the National Academy of Sciences of the United States of America1998
Conformational changes between the active-site and regulatory light chain of myosin as determined by luminescence resonance energy transfer: the effect of nucleotides and actin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 59 citations in OpenAlex.
- Conformational equilibrium of an ABC transporter analyzed by luminescence resonance energy transfer.Biophysical journal · 2025Article
- Asymmetric myosin binding to the thin filament as revealed by a fluorescent nanocircuit.Archives of biochemistry and biophysics · 2013Article
- Direct detection of adenosine in undiluted serum using a luminescent aptamer sensor attached to a terbium complex.Analytical chemistry · 2012Article
- Fluorescence applications in molecular neurobiology.Neuron · 2010Review
- Site-directed spectroscopic probes of actomyosin structural dynamics.Annual review of biophysics · 2009Review
- Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility.Structure (London, England : 1993) · 2007Article
- Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Myosin regulatory domain orientation in skeletal muscle fibers: application of novel electron paramagnetic resonance spectral decomposition and molecular modeling methods.Biophysical journal · 2004Article
- Holding two heads together: stability of the myosin II rod measured by resonance energy transfer between the heads.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Structural characterization of weakly attached cross-bridges in the A*M*ATP state in permeabilized rabbit psoas muscle.Biophysical journal · 2002Article
- Engineering a terbium-binding site into an integral membrane protein for luminescence energy transfer.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Conformational selection during weak binding at the actin and myosin interface.Biophysical journal · 2000Article
- Influence of ionic strength on the actomyosin reaction steps in contracting skeletal muscle fibers.Biophysical journal · 2000Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Myosin is thought to generate movement of actin filaments via a conformational change between its light-chain domain and its catalytic domain that is driven by the binding of nucleotides and actin. To monitor this change, we have measured distances between a gizzard regulatory light chain (Cys 108) and the active site (near or at Trp 130) of skeletal myosin subfragment 1 (S1) by using luminescence resonance energy transfer and a photoaffinity ATP-lanthanide analog. The technique allows relatively long distances to be measured, and the label enables site-specific attachment at the active-site with only modest affect on myosin's enzymology. The distance between these sites is 66.8 +/- 2.3 A when the nucleotide is ADP and is unchanged on binding to actin. The distance decreases slightly with ADP-BeF3, (-1.6 +/- 0.3 A) and more significantly with ADP-AlF4 (-4.6 +/- 0.2 A). During steady-state hydrolysis of ATP, the distance is temperature-dependent, becoming shorter as temperature increases and the complex with ADP.Pi is favored over that with ATP. We conclude that the distance between the active site and the light chain varies as Acto-S1-ADP approximately S1-ADP > S1-ADP-BeF3 > S1-ADP-AlF4 approximately S1-ADP-Pi and that S1-ATP > S1-ADP-Pi. The changes in distance are consistent with a substantial rotation of the light-chain binding domain of skeletal S1 between the prepowerstroke state, simulated by S1-ADP-AlF4, and the post-powerstroke state, simulated by acto-S1-ADP.
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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.