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1URQ

Crystal structure of neuronal Q-SNAREs in complex with R-SNARE motif of Tomosyn

1URQ の概要
エントリーDOI10.2210/pdb1urq/pdb
関連するPDBエントリー1BR0 1DN1 1EZ3 1HVV 1JTH 1KIL 1N7S 1SFC 2BU0
分子名称M-TOMOSYN ISOFORM, SYNTAXIN 1A, SYNAPTOSOMAL-ASSOCIATED PROTEIN 25, ... (5 entities in total)
機能のキーワードtransport protein, tomosyn-snare complex, exocytosis, four helical bundle, coiled coil
由来する生物種RATTUS NORVEGICUS (RAT)
詳細
タンパク質・核酸の鎖数4
化学式量合計32551.51
構造登録者
Pobbati, A.,Razeto, A.,Becker, S.,Fasshauer, D. (登録日: 2003-10-31, 公開日: 2004-08-26, 最終更新日: 2023-12-13)
主引用文献Pobbati, A.,Razeto, A.,Boddener, M.,Becker, S.,Fasshauer, D.
Structural Basis for the Inhibitory Role of Tomosyn in Exocytosis
J.Biol.Chem., 279:47192-, 2004
Cited by
PubMed Abstract: Upon Ca2+ influx synaptic vesicles fuse with the plasma membrane and release their neurotransmitter cargo into the synaptic cleft. Key players during this process are the Q-SNAREs syntaxin 1a and SNAP-25 and the R-SNARE synaptobrevin 2. It is thought that these membrane proteins gradually assemble into a tight trans-SNARE complex between vesicular and plasma membrane, ultimately leading to membrane fusion. Tomosyn is a soluble protein of 130 kDa that contains a COOH-terminal R-SNARE motif but lacks a transmembrane anchor. Its R-SNARE motif forms a stable core SNARE complex with syntaxin 1a and SNAP-25. Here we present the crystal structure of this core tomosyn SNARE complex at 2.0-A resolution. It consists of a four-helical bundle very similar to that of the SNARE complex containing synaptobrevin. Most differences are found on the surface, where they prevented tight binding of complexin. Both complexes form with similar rates as assessed by CD spectroscopy. In addition, synaptobrevin cannot displace the tomosyn helix from the tight complex and vice versa, indicating that both SNARE complexes represent end products. Moreover, data bank searches revealed that the R-SNARE motif of tomosyn is highly conserved throughout all eukaryotic kingdoms. This suggests that the formation of a tight SNARE complex is important for the function of tomosyn.
PubMed: 15316007
DOI: 10.1074/JBC.M408767200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 1urq
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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