Cited by 2,417Cellular transport and secretionLipid Membrane Structure and BehaviorNeuroscience and Neuropharmacology Research

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

Sutton, R. Bryan, Fasshauer, Dirk, Jahn, Reinhard, Brunger, Axel T.·1998·Nature

DOI 10.1038/26412

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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 A resolution of a core synaptic fusion complex containing syntaxin-1 A, 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 alpha-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.

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Authors: Sutton, R. B., Fasshauer, D., Jahn, R., & Brunger, A. T.
Affiliations: Howard Hughes Medical Institute (US)
Max Planck Society (DE)
ORCID: Sutton, R. Bryan
Fasshauer, Dirk
Jahn, Reinhard
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1998-09
Volume: 395
Issue: 6700
Pages: 347-353
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/26412
OpenAlex: W1822252127
Semantic Scholar: f0ea2581b47bed29546d2d208a47cff4312eb1fe
Cited by: 2,417
References: 52
Citations by year: 2026: 25 · 2025: 44 · 2024: 45 · 2023: 55 · 2022: 63 · 2021: 60 · 2020: 59 · 2019: 51 · 2018: 80 · 2017: 70 · 2016: 67 · 2015: 91 · 2014: 93 · 2013: 89 · 2012: 93
FWCI: 44.62
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords: SNARE complex, synaptic vesicle exocytosis, syntaxin 1A, membrane fusion, four-helix bundle, hydrophobic core, neurotransmitter release, vesicle fusion
MeSH terms: Antigens, Surface, Escherichia coli, Exocytosis, Membrane Fusion, Membrane Proteins, Models, Molecular, Nerve Tissue Proteins, Neurotoxins, Protein Binding, Protein Conformation, Recombinant Proteins, Synaptic Vesicles, Crystallography, X-Ray, Vesicular Transport Proteins, Macromolecular Substances, SNARE Proteins, R-SNARE Proteins, Synaptosomal-Associated Protein 25, Syntaxin 1

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

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