2LW9

NMR solution structure of Myo10 anti-CC

Summary for 2LW9

• Entry DOI: 10.2210/pdb2lw9/pdb
• NMR Information: BMRB: 18614
• Descriptor: Unconventionnal myosin-X (1 entity in total)
• Functional Keywords: myo10 anti-cc, motor protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytosol: Q9HD67
• Total number of polymer chains: 2
• Total formula weight: 12696.14

Authors

Ye, F.,Lu, Q.,Zhang, M. (deposition date: 2012-07-25, release date: 2012-09-26, Last modification date: 2024-05-01)

Primary citation

Lu, Q.,Ye, F.,Wei, Z.,Wen, Z.,Zhang, M.
Antiparallel coiled-coil-mediated dimerization of myosin X
Proc.Natl.Acad.Sci.USA, 109:17388-17393, 2012

PubMed 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 α-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.

PubMed: 23012428
DOI: 10.1073/pnas.1208642109

Experimental method

SOLUTION NMR