5OWO

Human cytoplasmic Dynein N-Terminus dimerization domain at 1.8 Angstrom resolution

5OWO の概要

• エントリーDOI: 10.2210/pdb5owo/pdb
• 分子名称: Cytoplasmic dynein 1 heavy chain 1, GLYCEROL, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: dynein, heavy chain, dimerization domain, motor protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 90191.91

構造登録者

Urnavicius, L.,Lau, C.K.,Elshenawy, M.M.,Morales-Rios, E.,Motz, C.,Yildiz, A.,Carter, A.P. (登録日: 2017-09-01, 公開日: 2018-07-11, 最終更新日: 2024-10-16)

主引用文献

Urnavicius, L.,Lau, C.K.,Elshenawy, M.M.,Morales-Rios, E.,Motz, C.,Yildiz, A.,Carter, A.P.
Cryo-EM shows how dynactin recruits two dyneins for faster movement.
Nature, 554:202-206, 2018

PubMed Abstract: Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. Here we use electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased towards recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two dyneins. We find that the shift towards a double dynein complex increases both the force and speed of the microtubule motor. Our 3.5 Å resolution cryo-electron microscopy reconstruction of a dynein tail-dynactin-BICDR1 complex reveals how dynactin can act as a scaffold to coordinate two dyneins side-by-side. Our work provides a structural basis for understanding how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dynein-dynactin transport machine.

PubMed: 29420470
DOI: 10.1038/nature25462

実験手法

X-RAY DIFFRACTION (1.79 Å)