3J99

Structure of 20S supercomplex determined by single particle cryoelectron microscopy (State IIIb)

Summary for 3J99

• Entry DOI: 10.2210/pdb3j99/pdb
• Related: 3J94 3J95 3J96 3J97 3J98
• EMDB information: 6204 6205 6206 6207 6208 6209 6210
• Descriptor: Vesicle-fusing ATPase, Alpha-soluble NSF attachment protein, Vesicle-associated membrane protein 2, ... (5 entities in total)
• Functional Keywords: vesicle trafficking, hydrolase
• Biological source: Cricetulus griseus (Chinese hamster); More
• Total number of polymer chains: 13
• Total formula weight: 667281.63

Authors

Zhao, M.,Wu, S.,Cheng, Y.,Brunger, A.T. (deposition date: 2014-12-05, release date: 2015-01-28, Last modification date: 2024-02-21)

Primary citation

Zhao, M.,Wu, S.,Zhou, Q.,Vivona, S.,Cipriano, D.J.,Cheng, Y.,Brunger, A.T.
Mechanistic insights into the recycling machine of the SNARE complex.
Nature, 518:61-67, 2015

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-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.

PubMed: 25581794
DOI: 10.1038/nature14148

Experimental method

ELECTRON MICROSCOPY (8.2 Å)