6MDP
The D1 and D2 domain rings of NSF engaging the SNAP-25 N-terminus within the 20S supercomplex (focused refinement on D1/D2 rings, class 2)
Summary for 6MDP
| Entry DOI | 10.2210/pdb6mdp/pdb |
| EMDB information | 9103 |
| Descriptor | Vesicle-fusing ATPase, Synaptosomal-associated protein 25, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | snare, nsf, snap, atpase, aaa, disassembly, synapse, membrane fusion, exocytosis, hydrolase |
| Biological source | Cricetulus griseus (Chinese hamster) More |
| Total number of polymer chains | 7 |
| Total formula weight | 541986.78 |
| Authors | White, K.I.,Zhao, M.,Brunger, A.T. (deposition date: 2018-09-04, release date: 2018-09-19, Last modification date: 2024-03-13) |
| Primary citation | White, K.I.,Zhao, M.,Choi, U.B.,Pfuetzner, R.A.,Brunger, A.T. Structural principles of SNARE complex recognition by the AAA+ protein NSF. Elife, 7:-, 2018 Cited by PubMed Abstract: The recycling of SNARE proteins following complex formation and membrane fusion is an essential process in eukaryotic trafficking. A highly conserved AAA+ protein, NSF (-ethylmaleimide sensitive factor) and an adaptor protein, SNAP (soluble NSF attachment protein), disassemble the SNARE complex. We report electron-cryomicroscopy structures of the complex of NSF, αSNAP, and the full-length soluble neuronal SNARE complex (composed of syntaxin-1A, synaptobrevin-2, SNAP-25A) in the presence of ATP under non-hydrolyzing conditions at ~3.9 Å resolution. These structures reveal electrostatic interactions by which two αSNAP molecules interface with a specific surface of the SNARE complex. This interaction positions the SNAREs such that the 15 N-terminal residues of SNAP-25A are loaded into the D1 ring pore of NSF via a spiral pattern of interactions between a conserved tyrosine NSF residue and SNAP-25A backbone atoms. This loading process likely precedes ATP hydrolysis. Subsequent ATP hydrolysis then drives complete disassembly. PubMed: 30198481DOI: 10.7554/eLife.38888 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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