3J67

Structural mechanism of the dynein powerstroke (post-powerstroke state)

3J67 の概要

• エントリーDOI: 10.2210/pdb3j67/pdb
• 関連するPDBエントリー: 3J68 4AKI
• EMDBエントリー: 5757 5758
• 分子名称: Dynein motor domain (1 entity in total)
• 機能のキーワード: motor protein
• 由来する生物種: Strongylocentrotus purpuratus (purple sea urchin)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 262122.23

構造登録者

Lin, J.,Okada, K.,Raytchev, M.,Smith, M.C.,Nicastro, D. (登録日: 2013-12-22, 公開日: 2014-04-23, 最終更新日: 2024-02-21)

主引用文献

Lin, J.,Okada, K.,Raytchev, M.,Smith, M.C.,Nicastro, D.
Structural mechanism of the dynein power stroke.
Nat.Cell Biol., 16:479-485, 2014

PubMed Abstract: Dyneins are large microtubule motor proteins required for mitosis, intracellular transport and ciliary and flagellar motility. They generate force through a power-stroke mechanism, which is an ATP-consuming cycle of pre- and post-power-stroke conformational changes that cause relative motion between different dynein domains. However, key structural details of dynein's force generation remain elusive. Here, using cryo-electron tomography of intact, active (that is, beating), rapidly frozen sea urchin sperm flagella, we determined the in situ three-dimensional structures of all domains of both pre- and post-power-stroke dynein, including the previously unresolved linker and stalk of pre-power-stroke dynein. Our results reveal that the rotation of the head relative to the linker is the key action in dynein movement, and that there are at least two distinct pre-power-stroke conformations: pre-I (microtubule-detached) and pre-II (microtubule-bound). We provide three-dimensional reconstructions of native dyneins in three conformational states, in situ, allowing us to propose a molecular model of the structural cycle underlying dynein movement.

PubMed: 24727830
DOI: 10.1038/ncb2939

実験手法

ELECTRON MICROSCOPY (34 Å)