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5ET1

Crystal structure of Myo3b-ARB1 in complex with Espin1-AR

Summary for 5ET1
Entry DOI10.2210/pdb5et1/pdb
Related5ET0
DescriptorEspin, Myosin-IIIb, GLYCEROL, ... (4 entities in total)
Functional Keywordsunconventional myosin, complex, protein binding, protein binding-motor protein complex, protein binding/motor protein
Biological sourceMus musculus (Mouse)
More
Cellular locationCytoplasm, 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 chains4
Total formula weight84949.30
Authors
Liu, H.,Li, J.,liu, W.,Zhang, M. (deposition date: 2015-11-17, release date: 2016-02-03, Last modification date: 2023-11-08)
Primary citationLiu, 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: 26785147
DOI: 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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