Myosin V: Chemomechanical-coupling ratchet with load-induced mechanical slip.

ABSTRACT: A chemomechanical-network model for myosin V is presented on the basis of both the nucleotide-dependent binding affinity of the head to an actin filament (AF) and asymmetries and similarity relations among the chemical transitions due to an intramolecular strain of the leading and trailing heads. The model allows for branched chemomechanical cycles and takes into account not only two different force-generating mechanical transitions between states wherein the leading head is strongly bound and the trailing head is weakly bound to the AF but also load-induced mechanical-slip transitions between states in which both heads are strongly bound. The latter is supported by the fact that ATP-independent high-speed backward stepping has been observed for myosin V, although such motility has never b

SUBMITTER: Sumi T 

PROVIDER: S-EPMC5647391 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature