4kp3 | pdb_00004kp3

Crystal Structure of MyoVa-GTD in Complex with Two Cargos

spinqualitylabelsall models 4kp3, resolution 2.41Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4kp3 is a 6 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3wb8 Gene: Myo5a (LK3 transgenic mice), Rilpl2 (LK3 transgenic mice), Mlph (LK3 transgenic mice) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MYO5A_MOUSE] Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation. [MELPH_MOUSE] Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor protein MYO5A. [RIPL2_MOUSE] Involved in cell shape and neuronal morphogenesis, positively regulating the establishment and maintenance of dendritic spines. May activate RAC1 (By similarity). Publication Abstract from PubMed 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. Structural basis of cargo recognitions for class V myosins.,Wei Z, Liu X, Yu C, Zhang M Proc Natl Acad Sci U S A. 2013 Jun 24. PMID:23798443 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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