3HD7

HELICAL EXTENSION OF THE NEURONAL SNARE COMPLEX INTO THE MEMBRANE, spacegroup C 1 2 1

Summary for 3HD7

• Entry DOI: 10.2210/pdb3hd7/pdb
• Related: 3HD9
• Descriptor: Vesicle-associated membrane protein 2, Syntaxin-1A, Synaptosomal-associated protein 25, ... (6 entities in total)
• Functional Keywords: membrane protein, coiled-coil, 4-helical bundle, cell junction, cytoplasmic vesicle, membrane, phosphoprotein, synapse, synaptosome, transmembrane, neurotransmitter transport, transport, cell membrane, lipoprotein, palmitate, exocytosis
• Biological source: Rattus norvegicus (Rat); More
• Cellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein: P63045; Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein (By similarity): P32851; Cytoplasm, perinuclear region (By similarity): P60881 P60881
• Total number of polymer chains: 8
• Total formula weight: 81123.52

Authors

Stein, A.,Weber, G.,Wahl, M.C.,Jahn, R. (deposition date: 2009-05-07, release date: 2009-07-14, Last modification date: 2025-05-28)

Primary citation

Stein, A.,Weber, G.,Wahl, M.C.,Jahn, R.
Helical extension of the neuronal SNARE complex into the membrane
Nature, 460:525-528, 2009

PubMed Abstract: Neurotransmission relies on synaptic vesicles fusing with the membrane of nerve cells to release their neurotransmitter content into the synaptic cleft, a process requiring the assembly of several members of the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) family. SNAREs represent an evolutionarily conserved protein family that mediates membrane fusion in the secretory and endocytic pathways of eukaryotic cells. On membrane contact, these proteins assemble in trans between the membranes as a bundle of four alpha-helices, with the energy released during assembly being thought to drive fusion. However, it is unclear how the energy is transferred to the membranes and whether assembly is conformationally linked to fusion. Here, we report the X-ray structure of the neuronal SNARE complex, consisting of rat syntaxin 1A, SNAP-25 and synaptobrevin 2, with the carboxy-terminal linkers and transmembrane regions at 3.4 A resolution. The structure shows that assembly proceeds beyond the already known core SNARE complex, resulting in a continuous helical bundle that is further stabilized by side-chain interactions in the linker region. Our results suggest that the final phase of SNARE assembly is directly coupled to membrane merger.

PubMed: 19571812
DOI: 10.1038/nature08156

Experimental method

X-RAY DIFFRACTION (3.4 Å)