Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 62, Issue 13, Pages 1462-1477Publisher
BIRKHAUSER VERLAG AG
DOI: 10.1007/s00018-005-5015-5
Keywords
enzyme catalysis; chemomechanical coupling; protein docking; beta-sheet distortion; kinetic mechanism; motor protein
Categories
Funding
- Wellcome Trust Funding Source: Medline
Ask authors/readers for more resources
Sophisticated molecular genetic, biochemical and biophysical studies have been used to probe the molecular mechanism of actomyosin-based motility. Recent solution measurements, high-resolution structures of recombinant myosin motor domains, and lower resolution structures of the complex formed by filamentous actin and the myosin motor domain provide detailed insights into the mechanism of chemomechanical coupling in the actomyosin system. They show how small conformational changes are amplified by a lever-arm mechanism to a working stroke of several nanometres, explain the mechanism that governs the directionality of actin-based movement, and reveal a communication pathway between the nucleotide binding pocket and the actin-binding region that explains the reciprocal relationship between actin and nucleotide affinity. Here we focus on the interacting elements in the actomyosin system and the communication pathways in the myosin motor domain that respond to actin binding.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available