Cryo-EM structure of SNAP-SNARE assembly in 20S particle

被引：35

作者：

Zhou, Qiang ^{[1
]}

Huang, Xuan ^{[1
]}

Sun, Shan ^{[1
]}

Li, Xueming ^{[2
]}

Wang, Hong-Wei ^{[2
]}

Sui, Sen-Fang ^{[1
]}

机构：

[1] Tsinghua Univ, Sch Life Sci, Struct Biol Ctr, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R China

[2] Tsinghua Univ, Sch Life Sci, Struct Biol Ctr,Key Lab Prot Sci, Tsinghua Peking Joint Ctr Life Sci,Minist Educ, Beijing 100084, Peoples R China

来源：

CELL RESEARCH | 2015年 / 25卷 / 05期

基金：

中国国家自然科学基金;

关键词：

alpha-SNAP; NSF; cryo-EM; 20S particle; membrane fusion; SENSITIVE FUSION PROTEIN; CRYSTAL-STRUCTURE; ALPHA-SNAP; FACTOR NSF; TERMINAL DOMAIN; COMPLEX; BINDING; EXOCYTOSIS; RESOLUTION; NANODISCS;

D O I：

10.1038/cr.2015.47

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

N-ethylmaleimide-sensitive factor (NSF) and a soluble NSF attachment proteins (alpha-SNAPs) work together within a 20S particle to disassemble and recycle the SNAP receptor (SNARE) complex after intracellular membrane fusion. To understand the disassembly mechanism of the SNARE complex by NSF and alpha-SNAP, we performed single-particle cryo-electron microscopy analysis of 20S particles and determined the structure of the alpha-SNAP-SNARE assembly portion at a resolution of 7.35 angstrom. The structure illustrates that four alpha-SNAPs wrap around the single left-handed SNARE helical bundle as a right-handed cylindrical assembly within a 20S particle. A conserved hydrophobic patch connecting helices 9 and 10 of each alpha-SNAP forms a chock protruding into the groove of the SNARE four-helix bundle. Biochemical studies proved that this structural element was critical for SNARE complex disassembly. Our study suggests how four alpha-SNAPs may coordinate with the NSF to tear the SNARE complex into individual proteins.

引用

页码：551 / 560

页数：10

共 48 条

[1]

[Anonymous], 2014, Curr. Protoc. Bioinf.

[2] Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs [J].