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

Details

Serval ID
serval:BIB_AAB1EC3226CF
Type
Article: article from journal or magazin.
Collection
Publications
Title
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution.
Journal
Nature
Author(s)
Sutton R.B., Fasshauer D., Jahn R., Brunger A.T.
ISSN
0028-0836 (Print)
ISSN-L
0028-0836
Publication state
Published
Issued date
1998
Peer-reviewed
Oui
Volume
395
Number
6700
Pages
347-353
Language
english
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.
Keywords
Antigens, Surface/chemistry, Antigens, Surface/metabolism, Crystallography, X-Ray, Escherichia coli, Exocytosis, Macromolecular Substances, Membrane Fusion, Membrane Proteins/chemistry, Membrane Proteins/metabolism, Models, Molecular, Nerve Tissue Proteins/chemistry, Nerve Tissue Proteins/metabolism, Neurotoxins/metabolism, Protein Binding, Protein Conformation, R-SNARE Proteins, Recombinant Proteins/chemistry, Recombinant Proteins/metabolism, SNARE Proteins, Synaptic Vesicles/chemistry, Synaptic Vesicles/metabolism, Synaptosomal-Associated Protein 25, Syntaxin 1, Vesicular Transport Proteins
Pubmed
Web of science
Create date
15/09/2011 9:44
Last modification date
20/08/2019 15:14
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