Structural highlights
6mdo is a 7 chain structure with sequence from Buffalo rat and Cho cell lines. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , |
| Related: | 3j93, 3j94, 3j96, 3j97, 3j98, 3j99 |
| Gene: | NSF (CHO cell lines), Snap25, Snap (Buffalo rat) |
| Activity: | Vesicle-fusing ATPase, with EC number 3.6.4.6 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[NSF_CRIGR] Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seem to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin. Interaction with AMPAR subunit GRIA2 leads to influence GRIA2 membrane cycling. [SNP25_RAT] t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF.
Publication Abstract from PubMed
The recycling of SNARE proteins following complex formation and membrane fusion is an essential process in eukaryotic trafficking. A highly conserved AAA+ protein, NSF (N-ethylmaleimide sensitive factor) and an adaptor protein, SNAP (soluble NSF attachment protein), disassembles the SNARE complex. We report electron-cryomicroscopy structures of the complex of NSF, alphaSNAP, 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 A resolution. These structures reveal electrostatic interactions by which two alphaSNAP 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.
Structural principles of SNARE complex recognition by the AAA+ protein NSF.,White KI, Zhao M, Choi UB, Pfuetzner RA, Brunger AT Elife. 2018 Sep 10;7. pii: 38888. doi: 10.7554/eLife.38888. PMID:30198481[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ White KI, Zhao M, Choi UB, Pfuetzner RA, Brunger AT. Structural principles of SNARE complex recognition by the AAA+ protein NSF. Elife. 2018 Sep 10;7. pii: 38888. doi: 10.7554/eLife.38888. PMID:30198481 doi:http://dx.doi.org/10.7554/eLife.38888
