7MGM

Structure of yeast cytoplasmic dynein with AAA3 Walker B mutation bound to Lis1

7MGM の概要

• エントリーDOI: 10.2210/pdb7mgm/pdb
• EMDBエントリー: 23829
• 分子名称: dynein AAA3-WalkerB mutant (E2488Q), Nuclear distribution protein PAC1, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: motor, aaa, motor protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 447582.59

構造登録者

Lahiri, I.,Reimer, J.M.,Leschziner, A.E. (登録日: 2021-04-12, 公開日: 2022-01-19, 最終更新日: 2024-05-29)

主引用文献

Gillies, J.P.,Reimer, J.M.,Karasmanis, E.P.,Lahiri, I.,Htet, Z.M.,Leschziner, A.E.,Reck-Peterson, S.L.
Structural basis for cytoplasmic dynein-1 regulation by Lis1.
Elife, 11:-, 2022

PubMed Abstract: The lissencephaly 1 gene, , is mutated in patients with the neurodevelopmental disease lissencephaly. The Lis1 protein is conserved from fungi to mammals and is a key regulator of cytoplasmic dynein-1, the major minus-end-directed microtubule motor in many eukaryotes. Lis1 is the only dynein regulator known to bind directly to dynein's motor domain, and by doing so alters dynein's mechanochemistry. Lis1 is required for the formation of fully active dynein complexes, which also contain essential cofactors: dynactin and an activating adaptor. Here, we report the first high-resolution structure of the yeast dynein-Lis1 complex. Our 3.1 Å structure reveals, in molecular detail, the major contacts between dynein and Lis1 and between Lis1's ß-propellers. Structure-guided mutations in Lis1 and dynein show that these contacts are required for Lis1's ability to form fully active human dynein complexes and to regulate yeast dynein's mechanochemistry and in vivo function.

PubMed: 34994688
DOI: 10.7554/eLife.71229

実験手法

ELECTRON MICROSCOPY (3.1 Å)