Structural mechanism of the recovery stroke in the Myosin molecular motor
- 29 April 2005
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 102 (19) , 6873-6878
- https://doi.org/10.1073/pnas.0408784102
Abstract
The power stroke pulling myosin along actin filaments during muscle contraction is achieved by a large rotation (≈60°) of the myosin lever arm after ATP hydrolysis. Upon binding the next ATP, myosin dissociates from actin, but its ATPase site is still partially open and catalytically off. Myosin must then close and activate its ATPase site while returning the lever arm for the next power stroke. A mechanism for this coupling between the ATPase site and the distant lever arm is determined here by generating a continuous series of optimized intermediates between the crystallographic end-states of the recovery stroke. This yields a detailed structural model for communication between the catalytic and the force-generating regions that is consistent with experimental observations. The coupling is achieved by an amplifying cascade of conformational changes along the relay helix lying between the ATPase and the domain carrying the lever arm.Keywords
This publication has 28 references indexed in Scilit:
- Automated computation of low‐energy pathways for complex rearrangements in proteins: Application to the conformational switch of Ras p21Proteins-Structure Function and Bioinformatics, 2005
- Mechanism of Primary Proton Transfer in BacteriorhodopsinStructure, 2004
- A structural state of the myosin V motor without bound nucleotideNature, 2003
- The Myosin Relay Helix to Converter Interface Remains Intact throughout the Actomyosin ATPase CycleJournal of Biological Chemistry, 2001
- SURVEY AND SUMMARY: The morph server: a standardized system for analyzing and visualizing macromolecular motions in a database frameworkNucleic Acids Research, 2000
- Structural Mechanism of Muscle ContractionAnnual Review of Biochemistry, 1999
- Simulation of activation free energies in molecular systemsThe Journal of Chemical Physics, 1996
- VMD: Visual molecular dynamicsJournal of Molecular Graphics, 1996
- Targeted molecular dynamics: A new approach for searching pathways of conformational transitionsJournal of Molecular Graphics, 1994
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983