1JTH

Crystal structure and biophysical properties of a complex between the N-terminal region of SNAP25 and the SNARE region of syntaxin 1a

1JTH の概要

• エントリーDOI: 10.2210/pdb1jth/pdb
• 関連するPDBエントリー: 1DN1 1HVV 1SFC
• 分子名称: SNAP25, syntaxin 1a (3 entities in total)
• 機能のキーワード: coiled-coil, polar layer, endocytosis-exocytosis complex, endocytosis/exocytosis
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 37256.14

構造登録者

Misura, K.M.S.,Gonzalez Jr., L.C.,May, A.P.,Scheller, R.H.,Weis, W.I. (登録日: 2001-08-21, 公開日: 2001-11-28, 最終更新日: 2024-03-13)

主引用文献

Misura, K.M.,Gonzalez Jr., L.C.,May, A.P.,Scheller, R.H.,Weis, W.I.
Crystal structure and biophysical properties of a complex between the N-terminal SNARE region of SNAP25 and syntaxin 1a.
J.Biol.Chem., 276:41301-41309, 2001

PubMed Abstract: SNARE proteins are required for intracellular membrane fusion. In the neuron, the plasma membrane SNAREs syntaxin 1a and SNAP25 bind to VAMP2 found on neurotransmitter-containing vesicles. These three proteins contain "SNARE regions" that mediate their association into stable tetrameric coiled-coil structures. Syntaxin 1a contributes one such region, designated H3, and SNAP25 contributes two SNARE regions to the fusogenic complex with VAMP2. Syntaxin 1a H3 (syn1aH3) and SNAP25 can form a stable assembly, which can then be bound by VAMP2 to form the full SNARE complex. Here we show that syn1aH3 can also form a stable but kinetically trapped complex with the N-terminal SNARE region of SNAP25 (S25N). The crystal structure of this complex reveals an extended parallel four-helix bundle similar to that of the core SNARE and the syn1aH3-SNAP25 complexes. The inherent ability of syn1aH3 and S25N to associate stably in vitro implies that the intracellular fusion machinery must prevent formation of, or remove, any non-productive complexes. Comparison with the syn1aH3-SNAP25 complex suggests that the linkage of the N- and C-terminal SNAP25 SNARE regions is kinetically advantageous in preventing formation of the non-productive syn1aH3-S25N complex. We also demonstrate that the syn1aH3-S25N complex can be disassembled by alpha-SNAP and N-ethylmaleimide-sensitive factor.

PubMed: 11533035
DOI: 10.1074/jbc.M106853200

実験手法

X-RAY DIFFRACTION (2 Å)