5ET0

Crystal structure of Myo3b-ARB2 in complex with Espin1-AR

5ET0 の概要

• エントリーDOI: 10.2210/pdb5et0/pdb
• 関連するPDBエントリー: 5ET1
• 分子名称: Espin, Myosin-IIIb (3 entities in total)
• 機能のキーワード: unconventional myosin, protein binding, signaling, protein binding-motor protein complex, protein binding/motor protein
• 由来する生物種: Mus musculus (Mouse); 詳細
• 細胞内の位置: 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
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 88304.93

構造登録者

Liu, H.,Li, J.,Liu, W.,Zhang, M. (登録日: 2015-11-17, 公開日: 2016-02-03, 最終更新日: 2023-11-08)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2.3 Å)