Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Mechanistic insights into the recycling machine of the SNARE complex.
Journal, issue, pages	Nature, Vol. 518, Issue 7537, Page 61-67, Year 2015
Publish date	Feb 5, 2015
Authors	Minglei Zhao / Shenping Wu / Qiangjun Zhou / Sandro Vivona / Daniel J Cipriano / Yifan Cheng / Axel T Brunger /
PubMed Abstract	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.
External links	Nature / PubMed:25581794 / PubMed Central
Methods	EM (single particle)
Resolution	4.2 - 8.4 Å
Structure data	6204 3j94 EMDB-6204, PDB-3j94: Structure of ATP-bound N-ethylmaleimide sensitive factor determined by single particle cryoelectron microscopy Method: EM (single particle) / Resolution: 4.2 Å 6205 3j95 EMDB-6205, PDB-3j95: Structure of ADP-bound N-ethylmaleimide sensitive factor determined by single particle cryoelectron microscopy Method: EM (single particle) / Resolution: 7.6 Å 6206 3j96 EMDB-6206: Structure of 20S supercomplex determined by single particle cryoelectron microscopy, state I PDB-3j96: Structure of 20S supercomplex determined by single particle cryoelectron microscopy (State I) Method: EM (single particle) / Resolution: 7.6 Å 6207 3j97 EMDB-6207: Structure of 20S supercomplex determined by single particle cryoelectron microscopy, state II PDB-3j97: Structure of 20S supercomplex determined by single particle cryoelectron microscopy (State II) Method: EM (single particle) / Resolution: 7.8 Å 6208 3j98 EMDB-6208: Structure of 20S supercomplex determined by single particle cryoelectron microscopy, state IIIa PDB-3j98: Structure of 20S supercomplex determined by single particle cryoelectron microscopy (State IIIa) Method: EM (single particle) / Resolution: 8.4 Å 6209 3j99 EMDB-6209: Structure of 20S supercomplex determined by single particle cryoelectron microscopy, state IIIb PDB-3j99: Structure of 20S supercomplex determined by single particle cryoelectron microscopy (State IIIb) Method: EM (single particle) / Resolution: 8.2 Å EMDB-6210: Structure of 20S supercomplex with V7-SNARE determined by single particle cryoelectron microscopy Method: EM (single particle) / Resolution: 8.0 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM
Source	cricetulus griseus (Chinese hamster) rattus norvegicus (Norway rat)
Keywords	HYDROLASE / ATPases associated with diverse cellular activities / vesicle trafficking