+検索条件
-Structure paper
タイトル | Mechanistic insights into the recycling machine of the SNARE complex. |
---|---|
ジャーナル・号・ページ | Nature, Vol. 518, Issue 7537, Page 61-67, Year 2015 |
掲載日 | 2015年2月5日 |
著者 | Minglei Zhao / Shenping Wu / Qiangjun Zhou / Sandro Vivona / Daniel J Cipriano / Yifan Cheng / Axel T Brunger / |
PubMed 要旨 | Evolutionarily conserved SNARE (soluble N-ethylmaleimide sensitive factor attachment protein receptors) proteins form a complex that drives membrane fusion in eukaryotes. The ATPase NSF (N- ...Evolutionarily conserved SNARE (soluble N-ethylmaleimide sensitive factor attachment protein receptors) proteins form a complex that drives membrane fusion in eukaryotes. The ATPase NSF (N-ethylmaleimide sensitive factor), together with SNAPs (soluble NSF attachment protein), disassembles the SNARE complex into its protein components, making individual SNAREs available for subsequent rounds of fusion. Here we report structures of ATP- and ADP-bound NSF, and the NSF/SNAP/SNARE (20S) supercomplex determined by single-particle electron cryomicroscopy at near-atomic to sub-nanometre resolution without imposing symmetry. Large, potentially force-generating, conformational differences exist between ATP- and ADP-bound NSF. The 20S supercomplex exhibits broken symmetry, transitioning from six-fold symmetry of the NSF ATPase domains to pseudo four-fold symmetry of the SNARE complex. SNAPs interact with the SNARE complex with an opposite structural twist, suggesting an unwinding mechanism. The interfaces between NSF, SNAPs, and SNAREs exhibit characteristic electrostatic patterns, suggesting how one NSF/SNAP species can act on many different SNARE complexes. |
リンク | Nature / PubMed:25581794 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 4.2 - 8.4 Å |
構造データ | EMDB-6204, PDB-3j94: EMDB-6205, PDB-3j95: EMDB-6206: Structure of 20S supercomplex determined by single particle cryoelectron microscopy, state I EMDB-6207: Structure of 20S supercomplex determined by single particle cryoelectron microscopy, state II EMDB-6208: Structure of 20S supercomplex determined by single particle cryoelectron microscopy, state IIIa EMDB-6209: Structure of 20S supercomplex determined by single particle cryoelectron microscopy, state IIIb EMDB-6210: |
化合物 | ChemComp-ATP: ChemComp-ADP: |
由来 |
|
キーワード | HYDROLASE / ATPases associated with diverse cellular activities / vesicle trafficking |