3J99

Structure of 20S supercomplex determined by single particle cryoelectron microscopy (State IIIb)

3J99 の概要

• エントリーDOI: 10.2210/pdb3j99/pdb
• 関連するPDBエントリー: 3J94 3J95 3J96 3J97 3J98
• EMDBエントリー: 6204 6205 6206 6207 6208 6209 6210
• 分子名称: Vesicle-fusing ATPase, Alpha-soluble NSF attachment protein, Vesicle-associated membrane protein 2, ... (5 entities in total)
• 機能のキーワード: vesicle trafficking, hydrolase
• 由来する生物種: Cricetulus griseus (Chinese hamster); 詳細
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 667281.63

構造登録者

Zhao, M.,Wu, S.,Cheng, Y.,Brunger, A.T. (登録日: 2014-12-05, 公開日: 2015-01-28, 最終更新日: 2024-02-21)

主引用文献

Zhao, M.,Wu, S.,Zhou, Q.,Vivona, S.,Cipriano, D.J.,Cheng, Y.,Brunger, A.T.
Mechanistic insights into the recycling machine of the SNARE complex.
Nature, 518:61-67, 2015

PubMed Abstract: Evolutionarily conserved SNARE (soluble N-ethylmaleimide sensitive factor attachment protein receptors) proteins form a complex that drives membrane fusion in eukaryotes. The ATPase NSF (N-ethylmaleimide sensitive factor), together with SNAPs (soluble NSF attachment protein), disassembles the SNARE complex into its protein components, making individual SNAREs available for subsequent rounds of fusion. Here we report structures of ATP- and ADP-bound NSF, and the NSF/SNAP/SNARE (20S) supercomplex determined by single-particle electron cryomicroscopy at near-atomic to sub-nanometre resolution without imposing symmetry. Large, potentially force-generating, conformational differences exist between ATP- and ADP-bound NSF. The 20S supercomplex exhibits broken symmetry, transitioning from six-fold symmetry of the NSF ATPase domains to pseudo four-fold symmetry of the SNARE complex. SNAPs interact with the SNARE complex with an opposite structural twist, suggesting an unwinding mechanism. The interfaces between NSF, SNAPs, and SNAREs exhibit characteristic electrostatic patterns, suggesting how one NSF/SNAP species can act on many different SNARE complexes.

PubMed: 25581794
DOI: 10.1038/nature14148

実験手法

ELECTRON MICROSCOPY (8.2 Å)