7DHW

Crystal structure of myosin-XI motor domain in complex with ADP-ALF4

7DHW の概要

• エントリーDOI: 10.2210/pdb7dhw/pdb
• 分子名称: Motor domain of myosin, MAGNESIUM ION, TETRAFLUOROALUMINATE ION, ... (6 entities in total)
• 機能のキーワード: myosin, motor domain, atpase, atp binding, motor protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 88424.08

構造登録者

Suzuki, K.,Haraguchi, T.,Tamanaha, M.,Yoshimura, K.,Imi, T.,Tominaga, M.,Sakayama, H.,Nishiyama, T.,Ito, K.,Murata, T. (登録日: 2020-11-17, 公開日: 2021-05-19, 最終更新日: 2023-11-29)

主引用文献

Haraguchi, T.,Tamanaha, M.,Suzuki, K.,Yoshimura, K.,Imi, T.,Tominaga, M.,Sakayama, H.,Nishiyama, T.,Murata, T.,Ito, K.
Discovery of ultrafast myosin, its amino acid sequence, and structural features.
Proc.Natl.Acad.Sci.USA, 119:-, 2022

PubMed Abstract: Cytoplasmic streaming with extremely high velocity (∼70 μm s) occurs in cells of the characean algae (). Because cytoplasmic streaming is caused by myosin XI, it has been suggested that a myosin XI with a velocity of 70 μm s, the fastest myosin measured so far, exists in cells. However, the velocity of the previously cloned myosin XI (XI) was about 20 μm s, one-third of the cytoplasmic streaming velocity in Recently, the genome sequence of has been published, revealing that this alga has four myosin XI genes. We cloned these four myosin XI (XI-1, 2, 3, and 4) and measured their velocities. While the velocities of XI-3 and XI-4 motor domains (MDs) were similar to that of XI MD, the velocities of XI-1 and XI-2 MDs were 3.2 times and 2.8 times faster than that of XI MD, respectively. The velocity of chimeric XI-1, a functional, full-length XI-1 construct, was 60 μm s These results suggest that XI-1 and XI-2 would be the main contributors to cytoplasmic streaming in cells and show that these myosins are ultrafast myosins with a velocity 10 times faster than fast skeletal muscle myosins in animals. We also report an atomic structure (2.8-Å resolution) of myosin XI using X-ray crystallography. Based on this crystal structure and the recently published cryo-electron microscopy structure of acto-myosin XI at low resolution (4.3-Å), it appears that the actin-binding region contributes to the fast movement of myosin XI. Mutation experiments of actin-binding surface loops support this hypothesis.

PubMed: 35173046
DOI: 10.1073/pnas.2120962119

実験手法

X-RAY DIFFRACTION (2.84 Å)