1SFC

NEURONAL SYNAPTIC FUSION COMPLEX

1SFC の概要

• エントリーDOI: 10.2210/pdb1sfc/pdb
• 分子名称: PROTEIN (SYNAPTOBREVIN 2), PROTEIN (SYNTAXIN 1A), PROTEIN (SNAP-25B), ... (7 entities in total)
• 機能のキーワード: membrane fusion protein complex, transport protein
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: 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
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 120945.06

構造登録者

Sutton, R.B.,Brunger, A.T. (登録日: 1998-08-24, 公開日: 1998-10-28, 最終更新日: 2024-02-14)

主引用文献

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

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: 9759724
DOI: 10.1038/26412

実験手法

X-RAY DIFFRACTION (2.4 Å)