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Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution

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  • R. Bryan Sutton

    (Yale University)

  • Dirk Fasshauer

    (Max-Planck-Institute for Biophysical Chemistry)

  • Reinhard Jahn

    (Max-Planck-Institute for Biophysical Chemistry)

  • Axel T. Brunger

    (Yale University)

Abstract

The evolutionarily conserved SNARE proteins and their complexes are involved in the fusion of vesicles with their target membranes; however, the overall organization and structural details of these complexes are unknown. Here we report the X-ray crystal structure at 2.4 Å resolution of a core synaptic fusion complex containing syntaxin-1A, synaptobrevin-II and SNAP-25B. The structure reveals a highly twisted and parallel four-helix bundle that differs from the bundles described for the haemagglutinin and HIV/SIV gp41 membrane-fusion proteins. Conserved leucine-zipper-like layers are found at the centre of the synaptic fusion complex. Embedded within these leucine-zipper layers is an ionic layer consisting of an arginine and three glutamine residues contributed from each of the four α-helices. These residues are highly conserved across the entire SNARE family. The regions flanking the leucine-zipper-like layers contain a hydrophobic core similar to that of more general four-helix-bundle proteins. The surface of the synaptic fusion complex is highly grooved and possesses distinct hydrophilic, hydrophobic and charged regions. These characteristics may be important for membrane fusion and for the binding of regulatory factors affecting neurotransmission.

Suggested Citation

  • R. Bryan Sutton & Dirk Fasshauer & Reinhard Jahn & Axel T. Brunger, 1998. "Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution," Nature, Nature, vol. 395(6700), pages 347-353, September.
    • Handle: RePEc:nat:nature:v:395:y:1998:i:6700:d:10.1038_26412
    DOI: 10.1038/26412
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    Cited by:

    1. Hong Huang & Qinqin Ouyang & Min Zhu & Haijia Yu & Kunrong Mei & Rong Liu, 2021. "mTOR-mediated phosphorylation of VAMP8 and SCFD1 regulates autophagosome maturation," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    2. B. U. Klink & A. Alavizargar & K. S. Kalyankumar & M. Chen & A. Heuer & C. Gatsogiannis, 2024. "Structural basis of α-latrotoxin transition to a cation-selective pore," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    3. Daungruthai Jarukanont & Imelda Bonifas Arredondo & Ricardo Femat & Martin E Garcia, 2015. "Vesicle Motion during Sustained Exocytosis in Chromaffin Cells: Numerical Model Based on Amperometric Measurements," PLOS ONE, Public Library of Science, vol. 10(12), pages 1-25, December.

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