6IP2

NSF-D1D2 part in the whole 20S complex

6IP2 の概要

• エントリーDOI: 10.2210/pdb6ip2/pdb
• EMDBエントリー: 9698
• 分子名称: Vesicle-fusing ATPase, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total)
• 機能のキーワード: membrane fusion, atpase, hydrolase
• 由来する生物種: Cricetulus griseus (Chinese hamster)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 518732.97

構造登録者

Huang, X.,Sun, S.,Wang, X.,Fan, F.,Zhou, Q.,Sui, S.F. (登録日: 2018-11-01, 公開日: 2019-04-24, 最終更新日: 2024-03-27)

主引用文献

Huang, X.,Sun, S.,Wang, X.,Fan, F.,Zhou, Q.,Lu, S.,Cao, Y.,Wang, Q.W.,Dong, M.Q.,Yao, J.,Sui, S.F.
Mechanistic insights into the SNARE complex disassembly.
Sci Adv, 5:eaau8164-eaau8164, 2019

PubMed Abstract: NSF (-ethylmaleimide-sensitive factor) and α-SNAP (α-soluble NSF attachment protein) bind to the SNARE (soluble NSF attachment protein receptor) complex, the minimum machinery to mediate membrane fusion, to form a 20S complex, which disassembles the SNARE complex for reuse. We report the cryo-EM structures of the α-SNAP-SNARE subcomplex and the NSF-D1D2 domain in the 20S complex at 3.9- and 3.7-Å resolutions, respectively. Combined with the biochemical and electrophysiological analyses, we find that α-SNAPs use R116 through electrostatic interactions and L197 through hydrophobic interactions to apply force mainly on two positions of the VAMP protein to execute disassembly process. Furthermore, we define the interaction between the amino terminus of the SNARE helical bundle and the pore loop of the NSF-D1 domain and demonstrate its essential role as a potential anchor for SNARE complex disassembly. Our studies provide a rotation model of α-SNAP-mediated disassembly of the SNARE complex.

PubMed: 30989110
DOI: 10.1126/sciadv.aau8164

実験手法

ELECTRON MICROSCOPY (3.7 Å)