6OIF

Cryo-EM structure of human TorsinA filament

これはPDB形式変換不可エントリーです。

6OIF の概要

• エントリーDOI: 10.2210/pdb6oif/pdb
• EMDBエントリー: 20076
• 分子名称: Torsin-1A, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total)
• 機能のキーワード: aaa+ atpase, nucleotide binding, nuclear envelope, endoplasmic reticulum, membrane, hydrolase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 25
• 化学式量合計: 827435.72

構造登録者

Zheng, W.,Demircioglu, F.E.,Schwartz, T.U.,Egelman, E.H. (登録日: 2019-04-09, 公開日: 2019-07-24, 最終更新日: 2024-11-13)

主引用文献

Demircioglu, F.E.,Zheng, W.,McQuown, A.J.,Maier, N.K.,Watson, N.,Cheeseman, I.M.,Denic, V.,Egelman, E.H.,Schwartz, T.U.
The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn.
Nat Commun, 10:3262-3262, 2019

PubMed Abstract: TorsinA is an ER-resident AAA + ATPase, whose deletion of glutamate E303 results in the genetic neuromuscular disease primary dystonia. TorsinA is an unusual AAA + ATPase that needs an external activator. Also, it likely does not thread a peptide substrate through a narrow central channel, in contrast to its closest structural homologs. Here, we examined the oligomerization of TorsinA to get closer to a molecular understanding of its still enigmatic function. We observe TorsinA to form helical filaments, which we analyzed by cryo-electron microscopy using helical reconstruction. The 4.4 Å structure reveals long hollow tubes with a helical periodicity of 8.5 subunits per turn, and an inner channel of ~ 4 nm diameter. We further show that the protein is able to induce tubulation of membranes in vitro, an observation that may reflect an entirely new characteristic of AAA + ATPases. We discuss the implications of these observations for TorsinA function.

PubMed: 31332180
DOI: 10.1038/s41467-019-11194-w

実験手法

ELECTRON MICROSCOPY (4.4 Å)