4R8G

Crystal Structure of Myosin-1c tail in complex with Calmodulin

Summary for 4R8G

• Entry DOI: 10.2210/pdb4r8g/pdb
• Descriptor: Unconventional myosin-Ic, Calmodulin, SULFATE ION (3 entities in total)
• Functional Keywords: ef hand, ph domain, iq motif, myosin, ca2+ signaling, force sensing, calcium binding, lipid binding, plasma membrane, cytoskeleton, protein binding-calcium-binding protein complex, protein binding/calcium-binding protein
• Biological source: Mus musculus (mouse); More
• Total number of polymer chains: 4
• Total formula weight: 88563.31

Authors

Lu, Q.,Li, J.,Ye, F.,Zhang, M. (deposition date: 2014-09-02, release date: 2014-12-03, Last modification date: 2024-03-20)

Primary citation

Lu, Q.,Li, J.,Ye, F.,Zhang, M.
Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling.
Nat.Struct.Mol.Biol., 22:81-88, 2015

PubMed Abstract: Class I myosins can sense cellular mechanical forces and function as tension-sensitive anchors or transporters. How mechanical load is transduced from the membrane-binding tail to the force-generating head in myosin-1 is unknown. Here we determined the crystal structure of the entire tail of mouse myosin-1c in complex with apocalmodulin, showing that myosin-1c adopts a stable monomer conformation suited for force transduction. The lever-arm helix and the C-terminal extended PH domain of the motor are coupled by a stable post-IQ domain bound to calmodulin in a highly unusual mode. Ca(2+) binding to calmodulin induces major conformational changes in both IQ motifs and the post-IQ domain and increases flexibility of the myosin-1c tail. Our study provides a structural blueprint for the neck and tail domains of myosin-1 and expands the target binding modes of the master Ca(2+)-signal regulator calmodulin.

PubMed: 25437912
DOI: 10.1038/nsmb.2923

Experimental method

X-RAY DIFFRACTION (3.503 Å)