ArticleBiophysical journal2005
Structural rearrangements in the active site of smooth-muscle myosin.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- EPR spectra and molecular dynamics agree that the nucleotide pocket of myosin V is closed and that it opens on binding actin.Journal of molecular biology · 2011Article
- Loop 1 dynamics in smooth muscle myosin: isoform specific differences modulate ADP release.Journal of muscle research and cell motility · 2011Article
- Switch I closure simultaneously promotes strong binding to actin and ADP in smooth muscle myosin.The Journal of biological chemistry · 2011Article
- Multiple conformations of the nucleotide site of Kinesin family motors in the triphosphate state.Journal of molecular biology · 2011Article
- Kinetics and thermodynamics of the rate-limiting conformational change in the actomyosin V mechanochemical cycle.Journal of molecular biology · 2011Article
- Nucleotide pocket thermodynamics measured by EPR reveal how energy partitioning relates myosin speed to efficiency.Journal of molecular biology · 2011Article
- Nucleotide-dependent conformational states of actin.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Site-directed spectroscopic probes of actomyosin structural dynamics.Annual review of biophysics · 2009Review
- 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
- Dynamics of the nucleotide pocket of myosin measured by spin-labeled nucleotides.Biophysical journal · 2007Article
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Authors and funding
4 authors.
Funding
Abstract
Structural rearrangements of the myosin upper-50 kD subdomain are thought to play a key role in coordinating actin binding with nucleotide hydrolysis during the myosin ATPase cycle. Such rearrangements could open and close the active site in opposition to the actin-binding cleft, helping explain the opposing affinities of myosin for actin and nucleotide. To directly examine conformational changes across the active site during the ATPase cycle we have genetically engineered a mutant of chicken smooth-muscle myosin, F344W motor domain essential light chain, which contains a single tryptophan (344W) located on a short loop between two alpha helixes that traverse the upper-50 kD subdomain in front of the active site. Fluorescence resonance energy transfer was examined between the 344W donor probe and 2'(3')-O-(N-methylanthraniloyl) (mant)-nucleotide acceptor probes in the active site of this construct. The observed fluorescence resonance energy transfer efficiencies were 6.4% in the presence of mant ADP and 23.8% in the presence of mant ATP, corresponding to distances of 33.4 A and 24.9 A, respectively. Our results are consistent with structural rearrangements in which there is an 8.5-A closure between the 344W residue and the mant moiety during the transition from the strongly (ADP) to weakly (ATP) actin-bound states of the myosin ATPase cycle.
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