2dfs
From Proteopedia
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[[Image:2dfs.gif|left|200px]] | [[Image:2dfs.gif|left|200px]] | ||
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'''3-D structure of Myosin-V inhibited state''' | '''3-D structure of Myosin-V inhibited state''' | ||
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[[Category: Taylor, K A.]] | [[Category: Taylor, K A.]] | ||
[[Category: Trybus, K M.]] | [[Category: Trybus, K M.]] | ||
- | [[Category: | + | [[Category: Calmodulin]] |
- | [[Category: | + | [[Category: Cryoelectron tomography]] |
- | [[Category: | + | [[Category: Inhibited state]] |
- | [[Category: | + | [[Category: Myosin-v]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:19:58 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 21:19, 3 May 2008
3-D structure of Myosin-V inhibited state
Overview
Unconventional myosin V (myoV) is an actin-based molecular motor that has a key function in organelle and mRNA transport, as well as in membrane trafficking. MyoV was the first member of the myosin superfamily shown to be processive, meaning that a single motor protein can 'walk' hand-over-hand along an actin filament for many steps before detaching. Full-length myoV has a low actin-activated MgATPase activity at low [Ca2+], whereas expressed constructs lacking the cargo-binding domain have a high activity regardless of [Ca2+] (refs 5-7). Hydrodynamic data and electron micrographs indicate that the active state is extended, whereas the inactive state is compact. Here we show the first three-dimensional structure of the myoV inactive state. Each myoV molecule consists of two heads that contain an amino-terminal motor domain followed by a lever arm that binds six calmodulins. The heads are followed by a coiled-coil dimerization domain (S2) and a carboxy-terminal globular cargo-binding domain. In the inactive structure, bending of myoV at the head-S2 junction places the cargo-binding domain near the motor domain's ATP-binding pocket, indicating that ATPase inhibition might occur through decreased rates of nucleotide exchange. The actin-binding interfaces are unobstructed, and the lever arm is oriented in a position typical of strong actin-binding states. This structure indicates that motor recycling after cargo delivery might occur through transport on actively treadmilling actin filaments rather than by diffusion.
About this Structure
2DFS is a Protein complex structure of sequences from Gallus gallus and Mus musculus. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography., Liu J, Taylor DW, Krementsova EB, Trybus KM, Taylor KA, Nature. 2006 Jul 13;442(7099):208-11. Epub 2006 Apr 16. PMID:16625208 Page seeded by OCA on Sun May 4 00:19:58 2008