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
-
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
-
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
-
[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.
-
[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.
Cited by
-
Activity of the SNARE Protein SNAP29 at the Endoplasmic Reticulum and Golgi Apparatus.Front Cell Dev Biol. 2021 Feb 18;9:637565. doi: 10.3389/fcell.2021.637565. eCollection 2021. Front Cell Dev Biol. 2021. PMID: 33718375 Free PMC article.
-
Structure of the flotillin complex in a native membrane environment.Proc Natl Acad Sci U S A. 2024 Jul 16;121(29):e2409334121. doi: 10.1073/pnas.2409334121. Epub 2024 Jul 10. Proc Natl Acad Sci U S A. 2024. PMID: 38985763 Free PMC article.
-
Conventional and Unconventional Protein Secretion in Yeast and Animal Cells.Methods Mol Biol. 2024;2841:1-17. doi: 10.1007/978-1-0716-4059-3_1. Methods Mol Biol. 2024. PMID: 39115761 Review.
-
Syntaxin opening by the MUN domain underlies the function of Munc13 in synaptic-vesicle priming.Nat Struct Mol Biol. 2015 Jul;22(7):547-54. doi: 10.1038/nsmb.3038. Epub 2015 Jun 1. Nat Struct Mol Biol. 2015. PMID: 26030875 Free PMC article.
-
All three components of the neuronal SNARE complex contribute to secretory vesicle docking.J Cell Biol. 2012 Aug 6;198(3):323-30. doi: 10.1083/jcb.201106158. J Cell Biol. 2012. PMID: 22869597 Free PMC article.
Publication types
MeSH terms
Substances
Associated data
- Actions
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
