3WB8

Crystal Structure of MyoVa-GTD

Summary for 3WB8

• Entry DOI: 10.2210/pdb3wb8/pdb
• Related: 4KP3
• Descriptor: Unconventional myosin-Va, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: helix bundle, motor protein
• Biological source: Mus musculus (mouse)
• Total number of polymer chains: 8
• Total formula weight: 370344.02

Authors

Wei, Z.,Liu, X.,Yu, C.,Zhang, M. (deposition date: 2013-05-13, release date: 2013-07-10, Last modification date: 2024-03-20)

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

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: 23798443
DOI: 10.1073/pnas.1306768110

Experimental method

X-RAY DIFFRACTION (2.499 Å)