5ET1
Crystal structure of Myo3b-ARB1 in complex with Espin1-AR
Summary for 5ET1
| Entry DOI | 10.2210/pdb5et1/pdb |
| Related | 5ET0 |
| Descriptor | Espin, Myosin-IIIb, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | unconventional myosin, complex, protein binding, protein binding-motor protein complex, protein binding/motor protein |
| Biological source | Mus musculus (Mouse) More |
| Cellular location | Cytoplasm, cytoskeleton. Isoform 2: Cytoplasm, cytoskeleton. Isoform 3: Cytoplasm, cytoskeleton. Isoform 4: Cytoplasm, cytoskeleton. Isoform 5: Cytoplasm, cytoskeleton. Isoform 8: Cytoplasm, cytoskeleton: Q9ET47 Cytoplasm, cytoskeleton : Q1EG27 |
| Total number of polymer chains | 4 |
| Total formula weight | 84949.30 |
| Authors | |
| Primary citation | Liu, H.,Li, J.,Raval, M.H.,Yao, N.,Deng, X.,Lu, Q.,Nie, S.,Feng, W.,Wan, J.,Yengo, C.M.,Liu, W.,Zhang, M. Myosin III-mediated cross-linking and stimulation of actin bundling activity of Espin Elife, 5:-, 2016 Cited by PubMed Abstract: Class III myosins (Myo3) and actin-bundling protein Espin play critical roles in regulating the development and maintenance of stereocilia in vertebrate hair cells, and their defects cause hereditary hearing impairments. Myo3 interacts with Espin1 through its tail homology I motif (THDI), however it is not clear how Myo3 specifically acts through Espin1 to regulate the actin bundle assembly and stabilization. Here we discover that Myo3 THDI contains a pair of repeat sequences capable of independently and strongly binding to the ankyrin repeats of Espin1, revealing an unexpected Myo3-mediated cross-linking mechanism of Espin1. The structures of Myo3 in complex with Espin1 not only elucidate the mechanism of the binding, but also reveal a Myo3-induced release of Espin1 auto-inhibition mechanism. We also provide evidence that Myo3-mediated cross-linking can further promote actin fiber bundling activity of Espin1. PubMed: 26785147DOI: 10.7554/eLife.12856 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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