4BYF

Crystal structure of human Myosin 1c in complex with calmodulin in the pre-power stroke state

4BYF の概要

• エントリーDOI: 10.2210/pdb4byf/pdb
• 分子名称: UNCONVENTIONAL MYOSIN-IC, CALMODULIN, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, myo1c, glut4 exocytosis, atpase, motor protein
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Isoform 1: Cytoplasm. Isoform 2: Cytoplasm. Isoform 3: Nucleus, nucleoplasm: O00159; Cytoplasm, cytoskeleton, spindle: P62158
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 202745.69

構造登録者

Munnich, S.,Taft, M.H.,Pathan-Chhatbar, S.,Manstein, D.J. (登録日: 2013-07-19, 公開日: 2014-03-26, 最終更新日: 2023-12-20)

主引用文献

Munnich, S.,Taft, M.H.,Manstein, D.J.
Crystal Structure of Human Myosin 1C-the Motor in Glut4 Exocytosis: Implications for Ca(2+) Regulation and 14-3-3 Binding.
J.Mol.Biol., 426:2070-, 2014

PubMed Abstract: Myosin 1c (Myo1c) plays a key role in supporting motile events that underlie cell migration, vesicle trafficking, insulin-stimulated glucose uptake and hearing. Here, we present the crystal structure of the human Myo1c motor in complex with its light chain calmodulin. Our structure reveals tight interactions of the motor domain with calmodulin bound to the first IQ motif in the neck region. Several of the calmodulin residues contributing to this interaction are also involved in Ca(2+) binding. Contact residues in the motor domain are linked to the central β-sheet and the HO helix, suggesting a mechanism for communicating changes in Ca(2+) binding in the neck region to the actin and nucleotide binding regions of the motor domain. The structural context and the chemical environment of Myo1c mutations that are involved in sensorineural hearing loss in humans are described and their impact on motor function is discussed. We show that a construct consisting of the motor domain of Myo1c and the first IQ motif is sufficient to establish a tight interaction with 14-3-3β (KD=0.9 μM) and present the model of a double-headed Myo1c-14-3-3 complex. This complex has been implicated in the exocytosis of glucose transporter 4 storage vesicles during insulin-stimulated glucose uptake.

PubMed: 24636949
DOI: 10.1016/J.JMB.2014.03.004

実験手法

X-RAY DIFFRACTION (2.74 Å)