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Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
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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“Indeed modeling the four SNARE proteins (Ufe1, Use1, Sec20, and Sec22) that are known to mediate the fusion between Golgi-derived retrograde transport vesicles with ER (87), together resulted in a complex that resembles a typical SNARE complex (84) (fig. S26B, C).”
From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [84]
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“Membrane fusion requires the formation of a 4-helix bundle (called the SNARE complex) between the vesicle SNARE and the target membrane SNAREs (84,85).”
From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [84]
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“SNARE complex (Sutton et al., 1998).”
Self-citation
Metadata
- Authors
- Sutton, R. B., Fasshauer, D., Jahn, R., & Brunger, A. T.
- Affiliations
- Howard Hughes Medical Institute (US)
- Max Planck Society (DE)
- Venue
- Nature
- Published
- 1998-09
- Volume
- 395
- Issue
- 6700
- Pages
- 347-353
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- 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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