2LW9: NMR solution structure of Myo10 anti-CC

Citation:
Proc. Natl. Acad. Sci. U. S. A. (2012) 109 p.17388-17393
Abstract
Processive movements of unconventional myosins on actin filaments generally require motor dimerization. A commonly accepted myosin dimerization mechanism is via formation of a parallel coiled-coil dimer by a stretch of amino acid residues immediately carboxyl-terminal to the motor's lever-arm domain. Here, we discover that the predicted coiled-coil region of myosin X forms a highly stable, antiparallel coiled-coil dimer (anti-CC). Disruption of the anti-CC either by single-point mutations or by replacement of the anti-CC with a parallel coiled coil with a similar length compromised the filopodial induction activity of myosin X. We further show that the anti-CC and the single alpha-helical domain of myosin X are connected by a semirigid helical linker. The anti-CC-mediated dimerization may enable myosin X to walk on both single and bundled actin filaments.
PDB ID: 2LW9Download
MMDB ID: 103219
PDB Deposition Date: 2012/7/25
Updated in MMDB: 2012/09
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2LW9: dimeric; determined by author
Molecular Components in 2LW9
Label Count Molecule
Proteins (2 molecules)
2
Unconventionnal Myosin-x(Gene symbol: MYO10)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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