期刊
EMBO JOURNAL
卷 22, 期 17, 页码 4365-4374出版社
WILEY
DOI: 10.1093/emboj/cdg420
关键词
AAA ATPase; electron cryomicroscopy; FREALIGN; NSF; vesicle fusion
资金
- NIGMS NIH HHS [P01 GM062580, 1-P01-GM62580] Funding Source: Medline
- NIMH NIH HHS [1-R01-MH63105-01, R01 MH063105] Funding Source: Medline
N-ethyl maleimide sensitive factor (NSF) belongs to the AAA family of ATPases and is involved in a number of cellular functions, including vesicle fusion and trafficking of membrane proteins. We present the three-dimensional structure of the hydrolysis mutant E329Q of NSF complexed with an ATP-ADP mixture at 11 Angstrom resolution by electron cryomicroscopy and single-particle averaging of NSF.alpha-SNAP.SNARE complexes. The NSF domains D1 and D2 form hexameric rings that are arranged in a double-layered barrel. Our structure is more consistent with an antiparallel orientation of the two rings rather than a parallel one. The crystal structure of the D2 domain of NSF was docked into the EM density map and shows good agreement, including details at the secondary structural level. Six protrusions corresponding to the N domain of NSF (NSF-N) emerge from the sides of the D1 domain ring. The density corresponding to alpha-SNAP and SNAREs is located on the 6-fold axis of the structure, near the NSF-N domains. The density of the N domain is weak, suggesting conformational variability in this part of NSF.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据