2f6h
From Proteopedia
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| - | [[Image:2f6h.gif|left|200px]] | + | [[Image:2f6h.gif|left|200px]] |
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| - | '''Myosin V cargo binding domain''' | + | {{Structure |
| + | |PDB= 2f6h |SIZE=350|CAPTION= <scene name='initialview01'>2f6h</scene>, resolution 2.25Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= MYO2, CDC66 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | }} | ||
| + | |||
| + | '''Myosin V cargo binding domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2F6H is a [ | + | 2F6H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F6H OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for myosin V discrimination between distinct cargoes., Pashkova N, Jin Y, Ramaswamy S, Weisman LS, EMBO J. 2006 Feb 22;25(4):693-700. Epub 2006 Jan 26. PMID:[http:// | + | Structural basis for myosin V discrimination between distinct cargoes., Pashkova N, Jin Y, Ramaswamy S, Weisman LS, EMBO J. 2006 Feb 22;25(4):693-700. Epub 2006 Jan 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16437158 16437158] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: mysoin v; cargo binding; cargo transport; vacuole binding; secreatory vescile binding]] | [[Category: mysoin v; cargo binding; cargo transport; vacuole binding; secreatory vescile binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:48:40 2008'' |
Revision as of 14:48, 20 March 2008
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| , resolution 2.25Å | |||||||
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| Gene: | MYO2, CDC66 (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Myosin V cargo binding domain
Overview
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.
About this Structure
2F6H is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structural basis for myosin V discrimination between distinct cargoes., Pashkova N, Jin Y, Ramaswamy S, Weisman LS, EMBO J. 2006 Feb 22;25(4):693-700. Epub 2006 Jan 26. PMID:16437158
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