Unknown

Dataset Information

0

Structural principles of SNARE complex recognition by the AAA+ protein NSF.


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 (N-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, ?SNAP, 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 ?SNAP 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.

SUBMITTER: White KI 

PROVIDER: S-EPMC6160233 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structural principles of SNARE complex recognition by the AAA+ protein NSF.

White K Ian KI   Zhao Minglei M   Choi Ucheor B UB   Pfuetzner Richard A RA   Brunger Axel T AT  

eLife 20180910


The recycling of SNARE proteins following complex formation and membrane fusion is an essential process in eukaryotic trafficking. A highly conserved AAA+ protein, NSF (<i>N</i>-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  ...[more]

Similar Datasets

| S-EPMC3750193 | biostudies-literature
| S-EPMC6873166 | biostudies-literature
| S-EPMC4441202 | biostudies-literature
| S-EPMC3137076 | biostudies-literature
| S-EPMC2797252 | biostudies-literature
| S-EPMC3682559 | biostudies-literature
| S-EPMC3382979 | biostudies-literature
| S-EPMC3979417 | biostudies-literature
| S-EPMC5415569 | biostudies-literature
| S-EPMC10461460 | biostudies-literature