- EMDB-3703: Human cytoplasmic dynein-1 tail in the twisted state -
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データベース: EMDB / ID: EMD-3703
タイトル
Human cytoplasmic dynein-1 tail in the twisted state
マップデータ
Tail region particles were recentered and extracted from the complete human dynein-1 complex. Particles predominantly contain the dynein heavy chain N-terminus in a twisted conformation.
試料
複合体: Human cytoplasmic dynein-1 tail in the twisted N-terminus state
ジャーナル: Cell / 年: 2017 タイトル: Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated. 著者: Kai Zhang / Helen E Foster / Arnaud Rondelet / Samuel E Lacey / Nadia Bahi-Buisson / Alexander W Bird / Andrew P Carter / 要旨: Cytoplasmic dynein-1 binds dynactin and cargo adaptor proteins to form a transport machine capable of long-distance processive movement along microtubules. However, it is unclear why dynein-1 moves ...Cytoplasmic dynein-1 binds dynactin and cargo adaptor proteins to form a transport machine capable of long-distance processive movement along microtubules. However, it is unclear why dynein-1 moves poorly on its own or how it is activated by dynactin. Here, we present a cryoelectron microscopy structure of the complete 1.4-megadalton human dynein-1 complex in an inhibited state known as the phi-particle. We reveal the 3D structure of the cargo binding dynein tail and show how self-dimerization of the motor domains locks them in a conformation with low microtubule affinity. Disrupting motor dimerization with structure-based mutagenesis drives dynein-1 into an open form with higher affinity for both microtubules and dynactin. We find the open form is also inhibited for movement and that dynactin relieves this by reorienting the motor domains to interact correctly with microtubules. Our model explains how dynactin binding to the dynein-1 tail directly stimulates its motor activity.
ダウンロード / ファイル: emd_3703.map.gz / 形式: CCP4 / 大きさ: 11.4 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
注釈
Tail region particles were recentered and extracted from the complete human dynein-1 complex. Particles predominantly contain the dynein heavy chain N-terminus in a twisted conformation.