Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
- PMID: 9759724
- DOI: 10.1038/26412
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A 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.
Comment in
-
Membrane fusion. SNARE the rod, coil the complex.Nature. 1998 Sep 24;395(6700):328-9. doi: 10.1038/26354. Nature. 1998. PMID: 9759719 No abstract available.
Similar articles
-
[Roles of tomosyn in regulated synaptic vesicle fusion].Tanpakushitsu Kakusan Koso. 2009 Sep;54(12 Suppl):1647-53. Tanpakushitsu Kakusan Koso. 2009. PMID: 21089602 Review. Japanese. No abstract available.
-
[Proteins regulating neurotransmitter release of synaptic vesicles at nerve terminals].Sheng Li Ke Xue Jin Zhan. 2003 Jan;34(1):6-10. Sheng Li Ke Xue Jin Zhan. 2003. PMID: 12778801 Review. Chinese.
-
Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs.Nat Struct Biol. 2002 Feb;9(2):107-11. doi: 10.1038/nsb746. Nat Struct Biol. 2002. PMID: 11786915
-
Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex.Nature. 2000 Mar 23;404(6776):355-62. doi: 10.1038/35006120. Nature. 2000. PMID: 10746715
-
Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly.Biochemistry. 1998 Jul 21;37(29):10354-62. doi: 10.1021/bi980542h. Biochemistry. 1998. PMID: 9671503
Cited by
-
Phosphorylation of Doc2 by EphB2 modulates Munc13-mediated SNARE complex assembly and neurotransmitter release.Sci Adv. 2024 May 17;10(20):eadi7024. doi: 10.1126/sciadv.adi7024. Epub 2024 May 17. Sci Adv. 2024. PMID: 38758791 Free PMC article.
-
Recent Developments in Engineering Non-Paralytic Botulinum Molecules for Therapeutic Applications.Toxins (Basel). 2024 Apr 3;16(4):175. doi: 10.3390/toxins16040175. Toxins (Basel). 2024. PMID: 38668600 Free PMC article. Review.
-
A hydrophobic groove in secretagogin allows for alternate interactions with SNAP-25 and syntaxin-4 in endocrine tissues.Proc Natl Acad Sci U S A. 2024 Apr 16;121(16):e2309211121. doi: 10.1073/pnas.2309211121. Epub 2024 Apr 9. Proc Natl Acad Sci U S A. 2024. PMID: 38593081 Free PMC article.
-
Molecular mechanism underlying SNARE-mediated membrane fusion enlightened by all-atom molecular dynamics simulations.Proc Natl Acad Sci U S A. 2024 Apr 16;121(16):e2321447121. doi: 10.1073/pnas.2321447121. Epub 2024 Apr 9. Proc Natl Acad Sci U S A. 2024. PMID: 38593076
-
Tomosyns attenuate SNARE assembly and synaptic depression by binding to VAMP2-containing template complexes.Nat Commun. 2024 Mar 26;15(1):2652. doi: 10.1038/s41467-024-46828-1. Nat Commun. 2024. PMID: 38531902 Free PMC article.
Publication types
MeSH terms
Substances
Associated data
- Actions
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases