Cellular and Molecular Life Sciences CMLS

, Volume 62, Issue 13, pp 1462–1477 | Cite as

Molecular mechanism of actomyosin-based motility

Review

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.

Key words.

Enzyme catalysis chemomechanical coupling protein docking β-sheet distortion kinetic mechanism motor protein 

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Copyright information

© Birkhäuser Verlag, Basel 2005

Authors and Affiliations

  1. 1.Department of BiosciencesUniversity of KentCanterburyUnited Kingdom
  2. 2.Institut für Biophysikalische Chemie, OE 4350Medizinische Hochschule HannoverHannoverGermany

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