title: Molecular mechanism of actomyosin-based motility.
abstract: 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.affiliation: Department of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, United Kingdom.
authors.forename: M A
authors.initials: MA
authors.lastname: Geeves
authors.forename: R
authors.initials: R
authors.lastname: Fedorov
authors.forename: D J
authors.initials: DJ
authors.lastname: Manstein
mesh_terms: D000199:Actins / Q000737:chemistry / Q000378:metabolism; D000205:Actomyosin / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D000818:Animals; D006801:Humans; D020409:Molecular Motor Proteins; D009068:Movement / Q000502:physiology*; D009218:Myosins / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins
chemical_list: D000199:Actins; D020409:Molecular Motor Proteins; D011994:Recombinant Proteins; D000205:Actomyosin; D009218:Myosins