1SFC
NEURONAL SYNAPTIC FUSION COMPLEX
Summary for 1SFC
| Entry DOI | 10.2210/pdb1sfc/pdb |
| Descriptor | PROTEIN (SYNAPTOBREVIN 2), PROTEIN (SYNTAXIN 1A), PROTEIN (SNAP-25B), ... (7 entities in total) |
| Functional Keywords | membrane fusion protein complex, transport protein |
| Biological source | Rattus norvegicus (Norway rat) More |
| Cellular location | Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein: P63045 Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein (By similarity): P32851 Cytoplasm, perinuclear region (By similarity): P60881 P60881 |
| Total number of polymer chains | 12 |
| Total formula weight | 120945.06 |
| Authors | Sutton, R.B.,Brunger, A.T. (deposition date: 1998-08-24, release date: 1998-10-28, Last modification date: 2024-02-14) |
| Primary citation | Sutton, R.B.,Fasshauer, D.,Jahn, R.,Brunger, A.T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature, 395:347-353, 1998 Cited by PubMed 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. PubMed: 9759724DOI: 10.1038/26412 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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