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Myosin V is a left-handed spiral motor on the right-handed actin helix.
- Source :
-
Nature structural biology [Nat Struct Biol] 2002 Jun; Vol. 9 (6), pp. 464-7. - Publication Year :
- 2002
-
Abstract
- Myosin V is a two-headed, actin-based molecular motor implicated in organelle transport. Previously, a single myosin V molecule has been shown to move processively along an actin filament in discrete approximately 36 nm steps. However, 36 nm is the helical repeat length of actin, and the geometry of the previous experiments may have forced the heads to bind to, or halt at, sites on one side of actin that are separated by 36 nm. To observe unconstrained motion, we suspended an actin filament in solution and attached a single myosin V molecule carrying a bead duplex. The duplex moved as a left-handed spiral around the filament, disregarding the right-handed actin helix. Our results indicate a stepwise walking mechanism in which myosin V positions and orients the unbound head such that the head will land at the 11th or 13th actin subunit on the opposing strand of the actin double helix.
- Subjects :
- Actins ultrastructure
Adenosine Triphosphate metabolism
Animals
Chick Embryo
Microspheres
Models, Molecular
Molecular Motor Proteins ultrastructure
Movement
Myosin Type V ultrastructure
Polystyrenes
Protein Structure, Quaternary
Protein Subunits
Rabbits
Rotation
Actins chemistry
Actins metabolism
Molecular Motor Proteins chemistry
Molecular Motor Proteins metabolism
Myosin Type V chemistry
Myosin Type V metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1072-8368
- Volume :
- 9
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Nature structural biology
- Publication Type :
- Academic Journal
- Accession number :
- 12006986
- Full Text :
- https://doi.org/10.1038/nsb803