6IP1

alpha-SNAP-SNARE subcomplex in the whole 20S complex

Summary for 6IP1

• Entry DOI: 10.2210/pdb6ip1/pdb
• EMDB information: 9697
• Descriptor: Vesicle-associated membrane protein 2, Syntaxin-1A, Synaptosomal-associated protein 25, ... (5 entities in total)
• Functional Keywords: membrane fusion, atpase, membrane protein
• Biological source: Rattus norvegicus (Rat); More
• Total number of polymer chains: 8
• Total formula weight: 199944.23

Authors

Huang, X.,Sun, S.,Wang, X.,Fan, F.,Zhou, Q.,Sui, S.F. (deposition date: 2018-11-01, release date: 2019-04-24, Last modification date: 2024-03-27)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.9 Å)