5BUZ

Crystal Structure of a Complex Between the SNARE Vam3 and the HOPS Vps33-Vps16 subcomplex from Chaetomium thermophilum

5BUZ の概要

• エントリーDOI: 10.2210/pdb5buz/pdb
• 関連するPDBエントリー: 4KMO 5BV0 5BV1
• 分子名称: SM (Sec1/Munc18-like) protein, Putative vacuolar protein sorting-associated protein, SNAP receptor-like protein (3 entities in total)
• 機能のキーワード: membrane trafficking, sm protein, hops complex, thermophile, snare domain, transport protein
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 238813.04

構造登録者

Baker, R.W.,Jeffrey, P.D.,Hughson, F.M. (登録日: 2015-06-04, 公開日: 2015-08-05, 最終更新日: 2023-09-27)

主引用文献

Baker, R.W.,Jeffrey, P.D.,Zick, M.,Phillips, B.P.,Wickner, W.T.,Hughson, F.M.
A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly.
Science, 349:1111-1114, 2015

PubMed Abstract: Fusion of intracellular transport vesicles requires soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) and Sec1/Munc18-family (SM) proteins. Membrane-bridging SNARE complexes are critical for fusion, but their spontaneous assembly is inefficient and may require SM proteins in vivo. We report x-ray structures of Vps33, the SM subunit of the yeast homotypic fusion and vacuole protein-sorting (HOPS) complex, bound to two individual SNAREs. The two SNAREs, one from each membrane, are held in the correct orientation and register for subsequent complex assembly. Vps33 and potentially other SM proteins could thus act as templates for generating partially zipped SNARE assembly intermediates. HOPS was essential to mediate SNARE complex assembly at physiological SNARE concentrations. Thus, Vps33 appears to catalyze SNARE complex assembly through specific SNARE motif recognition.

PubMed: 26339030
DOI: 10.1126/science.aac7906

実験手法

X-RAY DIFFRACTION (3.1 Å)