The cargo-binding domain regulates structure and activity of myosin 5

Article Abstract:

The structure of folded myosin 5, a two-headed motor protein that moves cargoes along actin filaments, and the role of the paired globular tail domains (GTDs) in regulating its activity are described. A combination of the results of electron microscopy analysis and motility assays show that without cargo, the GTDs bind in an intramolecular manner to the motor domains, producing an inhibited and compact structure that binds weakly to actin and allows the molecule to recycle towards new cargoes.

Analysis, Observations, Electron microscopy, Amino acid sequence, Amino acid sequencing, Properties, Structure

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Electron cyro-microscopy shows how strong binding of myosin to actin releases nucleotide

Article Abstract:

By fitting atomic models of actin and the myosin cross-bridge into high-resolution electron cryo-microscopy three-dimensional reconstructions, the molecular basis of muscle contraction is described.

Muscle contraction

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Two-headed binding of a processive myosin to F-Actin

Article Abstract:

A new study uses electron micrographs to support the 'hand-over-hand' mechanism for myosin V, abundant motor proteins that transport intracellular vesicles through interaction with actin filaments.

Cover Story

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