3VKH

X-ray structure of a functional full-length dynein motor domain

「3AY1」から置き換えられました

3VKH の概要

• エントリーDOI: 10.2210/pdb3vkh/pdb
• 関連するPDBエントリー: 3AY1 3VKG
• 分子名称: Dynein heavy chain, cytoplasmic, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• 機能のキーワード: aaa+ protein, molecular motor, microtubles, motor protein
• 由来する生物種: Dictyostelium discoideum (Slime mold)
• 細胞内の位置: Cytoplasm, cytoskeleton: P34036
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 772080.30

構造登録者

Kon, T.,Oyama, T.,Shimo-Kon, R.,Suto, K.,Kurisu, G. (登録日: 2011-11-16, 公開日: 2012-03-14, 最終更新日: 2023-11-08)

主引用文献

Kon, T.,Oyama, T.,Shimo-Kon, R.,Imamula, K.,Shima, T.,Sutoh, K.,Kurisu, G.
The 2.8 A crystal structure of the dynein motor domain
Nature, 484:345-350, 2012

PubMed Abstract: Dyneins are microtubule-based AAA(+) motor complexes that power ciliary beating, cell division, cell migration and intracellular transport. Here we report the most complete structure obtained so far, to our knowledge, of the 380-kDa motor domain of Dictyostelium discoideum cytoplasmic dynein at 2.8 Å resolution; the data are reliable enough to discuss the structure and mechanism at the level of individual amino acid residues. Features that can be clearly visualized at this resolution include the coordination of ADP in each of four distinct nucleotide-binding sites in the ring-shaped AAA(+) ATPase unit, a newly identified interaction interface between the ring and mechanical linker, and junctional structures between the ring and microtubule-binding stalk, all of which should be critical for the mechanism of dynein motility. We also identify a long-range allosteric communication pathway between the primary ATPase and the microtubule-binding sites. Our work provides a framework for understanding the mechanism of dynein-based motility.

PubMed: 22398446
DOI: 10.1038/nature10955

実験手法

X-RAY DIFFRACTION (3.8 Å)