6MDN

The 20S supercomplex engaging the SNAP-25 N-terminus (class 2)

Summary for 6MDN

• Entry DOI: 10.2210/pdb6mdn/pdb
• EMDB information: 9101
• Descriptor: Vesicle-fusing ATPase, Synaptosomal-associated protein 25, Syntaxin-1A, ... (7 entities in total)
• Functional Keywords: snare, nsf, snap, atpase, aaa, disassembly, synapse, membrane fusion, exocytosis, hydrolase
• Biological source: Cricetulus griseus (Chinese hamster); More
• Total number of polymer chains: 11
• Total formula weight: 655798.66

Authors

White, K.I.,Zhao, M.,Brunger, A.T. (deposition date: 2018-09-04, release date: 2018-09-19, Last modification date: 2024-03-13)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (4.4 Å)