4KP3
Crystal Structure of MyoVa-GTD in Complex with Two Cargos
Summary for 4KP3
Entry DOI | 10.2210/pdb4kp3/pdb |
Related | 3WB8 |
Descriptor | Unconventional myosin-Va, RILP-like protein 2, Melanophilin, ... (4 entities in total) |
Functional Keywords | helix bundle, motor protein-protein transport complex, motor protein/protein transport |
Biological source | Mus musculus (mouse) More |
Cellular location | Cytoplasm, cytosol : Q99LE1 Melanosome: Q91V27 |
Total number of polymer chains | 6 |
Total formula weight | 125193.13 |
Authors | |
Primary citation | Wei, Z.,Liu, X.,Yu, C.,Zhang, M. Structural basis of cargo recognitions for class V myosins Proc.Natl.Acad.Sci.USA, 110:11314-11319, 2013 Cited by PubMed Abstract: Class V myosins (MyoV), the most studied unconventional myosins, recognize numerous cargos mainly via the motor's globular tail domain (GTD). Little is known regarding how MyoV-GTD recognizes such a diverse array of cargos specifically. Here, we solved the crystal structures of MyoVa-GTD in its apo-form and in complex with two distinct cargos, melanophilin and Rab interacting lysosomal protein-like 2. The apo-MyoVa-GTD structure indicates that most mutations found in patients with Griscelli syndrome, microvillus inclusion disease, or cancers or in "dilute" rodents likely impair the folding of GTD. The MyoVa-GTD/cargo complex structure reveals two distinct cargo-binding surfaces, one primarily via charge-charge interaction and the other mainly via hydrophobic interactions. Structural and biochemical analysis reveal the specific cargo-binding specificities of various isoforms of mammalian MyoV as well as very different cargo recognition mechanisms of MyoV between yeast and higher eukaryotes. The MyoVa-GTD structures resolved here provide a framework for future functional studies of vertebrate class V myosins. PubMed: 23798443DOI: 10.1073/pnas.1306768110 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.405 Å) |
Structure validation
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