6MDP

The D1 and D2 domain rings of NSF engaging the SNAP-25 N-terminus within the 20S supercomplex (focused refinement on D1/D2 rings, class 2)

6MDP の概要

• エントリーDOI: 10.2210/pdb6mdp/pdb
• EMDBエントリー: 9103
• 分子名称: Vesicle-fusing ATPase, Synaptosomal-associated protein 25, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: snare, nsf, snap, atpase, aaa, disassembly, synapse, membrane fusion, exocytosis, hydrolase
• 由来する生物種: Cricetulus griseus (Chinese hamster); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 541986.78

構造登録者

White, K.I.,Zhao, M.,Brunger, A.T. (登録日: 2018-09-04, 公開日: 2018-09-19, 最終更新日: 2024-03-13)

主引用文献

White, K.I.,Zhao, M.,Choi, U.B.,Pfuetzner, R.A.,Brunger, A.T.
Structural principles of SNARE complex recognition by the AAA+ protein NSF.
Elife, 7:-, 2018

PubMed Abstract: The recycling of SNARE proteins following complex formation and membrane fusion is an essential process in eukaryotic trafficking. A highly conserved AAA+ protein, NSF (-ethylmaleimide sensitive factor) and an adaptor protein, SNAP (soluble NSF attachment protein), disassemble the SNARE complex. We report electron-cryomicroscopy structures of the complex of NSF, αSNAP, and the full-length soluble neuronal SNARE complex (composed of syntaxin-1A, synaptobrevin-2, SNAP-25A) in the presence of ATP under non-hydrolyzing conditions at ~3.9 Å resolution. These structures reveal electrostatic interactions by which two αSNAP molecules interface with a specific surface of the SNARE complex. This interaction positions the SNAREs such that the 15 N-terminal residues of SNAP-25A are loaded into the D1 ring pore of NSF via a spiral pattern of interactions between a conserved tyrosine NSF residue and SNAP-25A backbone atoms. This loading process likely precedes ATP hydrolysis. Subsequent ATP hydrolysis then drives complete disassembly.

PubMed: 30198481
DOI: 10.7554/eLife.38888

実験手法

ELECTRON MICROSCOPY (3.8 Å)