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 the adaptor protein SNAP (soluble NSF attachment protein), disassembles the SNARE complex, making individual SNAREs available for subsequent rounds of fusion. We determined structures of ATP- and ADP-bound NSF, and the NSF/SNAP/SNARE supercomplex (known as 20S particle) using single-particle cryo-electron microscopy (cryo-EM). We further dissected the mechanism of NSF mediated SNARE complex disassembly using single-molecule fluorescence microscopy based on the cryo-EM structures.
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