3H8D

Crystal structure of Myosin VI in complex with Dab2 peptide

Summary for 3H8D

• Entry DOI: 10.2210/pdb3h8d/pdb
• Descriptor: Myosin-VI, Disabled homolog 2, THIOCYANATE ION, ... (6 entities in total)
• Functional Keywords: myosin vi, myosin 6, dab2, cargo binding, protein-peptide complex, actin-binding, atp-binding, calmodulin-binding, cell projection, coated pit, coiled coil, cytoplasm, cytoplasmic vesicle, deafness, disease mutation, endocytosis, golgi apparatus, hearing, membrane, motor protein, myosin, nucleotide-binding, nucleus, phosphoprotein, protein transport, transport, alternative splicing, motor protein-signaling protein complex, motor protein/signaling protein
• Biological source: Mus musculus (mouse); More
• Cellular location: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q64331; Cytoplasmic vesicle, clathrin-coated vesicle membrane: O88797
• Total number of polymer chains: 8
• Total formula weight: 85991.69

Authors

Yu, C.,Feng, W.,Wei, Z.,Zhang, M. (deposition date: 2009-04-29, release date: 2009-09-29, Last modification date: 2024-03-20)

Primary citation

Yu, C.,Feng, W.,Wei, Z.,Miyanoiri, Y.,Wen, W.,Zhao, Y.,Zhang, M.
Myosin VI undergoes cargo-mediated dimerization
Cell(Cambridge,Mass.), 138:537-548, 2009

PubMed Abstract: Myosin VI is the only known molecular motor that moves toward the minus ends of actin filaments; thus, it plays unique roles in diverse cellular processes. The processive walking of myosin VI on actin filaments requires dimerization of the motor, but the protein can also function as a nonprocessive monomer. The molecular mechanism governing the monomer-dimer conversion is not clear. We report the high-resolution NMR structure of the cargo-free myosin VI cargo-binding domain (CBD) and show that it is a stable monomer in solution. The myosin VI CBD binds to a fragment of the clathrin-coated vesicle adaptor Dab2 with a high affinity, and the X-ray structure of the myosin VI CBD in complex with Dab2 reveals that the motor undergoes a cargo-binding-mediated dimerization. The cargo-binding-induced dimerization may represent a general paradigm for the regulation of processivity for myosin VI as well as other myosins, including myosin VII and myosin X.

PubMed: 19665975
DOI: 10.1016/j.cell.2009.05.030

Experimental method

X-RAY DIFFRACTION (2.2 Å)