2F6H

Myosin V cargo binding domain

Summary for 2F6H

• Entry DOI: 10.2210/pdb2f6h/pdb
• Descriptor: Myosin-2 (2 entities in total)
• Functional Keywords: mysoin v; cargo binding; cargo transport; vacuole binding; secreatory vescile binding, structural protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Bud neck: P19524
• Total number of polymer chains: 1
• Total formula weight: 47988.75

Authors

Pashkova, N.,Jin, Y.,Ramaswamy, S.,Weisman, L.S. (deposition date: 2005-11-29, release date: 2006-02-07, Last modification date: 2024-02-14)

Primary citation

Pashkova, N.,Jin, Y.,Ramaswamy, S.,Weisman, L.S.
Structural basis for myosin V discrimination between distinct cargoes
Embo J., 25:693-700, 2006

PubMed Abstract: Myosin V molecular motors move cargoes on actin filaments. A myosin V may move multiple cargoes to distinct places at different times. The cargoes attach to the globular tail of myosin V via cargo-specific receptors. Here we report the crystal structure at 2.2 A of the myosin V globular tail. The overall tertiary structure has not been previously observed. There are several patches of highly conserved regions distributed on the surface of the tail. These are candidate attachment sites for cargo-specific receptors. Indeed, we identified a region of five conserved surface residues that are solely required for vacuole inheritance. Likewise, we identified a region of five conserved surface residues that are required for secretory vesicle movement, but not vacuole movement. These two regions are at opposite ends of the oblong-shaped cargo-binding domain, and moreover are offset by 180 degrees. The fact that the cargo-binding areas are distant from each other and simultaneously exposed on the surface of the globular tail suggests that major targets for the regulation of cargo attachment are organelle-specific myosin V receptors.

PubMed: 16437158
DOI: 10.1038/sj.emboj.7600965

Experimental method

X-RAY DIFFRACTION (2.25 Å)