6ip1 | pdb_00006ip1

alpha-SNAP-SNARE subcomplex in the whole 20S complex

spinqualitylabelsall models 6ip1, resolution 3.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ip1 is a 8 chain structure with sequence from Bovin and Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: Vamp2 (Buffalo rat), Stx1a (Buffalo rat), Snap25 (Buffalo rat), NAPA (BOVIN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [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. [VAMP2_RAT] Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). [STX1A_RAT] Potentially involved in docking of synaptic vesicles at presynaptic active zones. May play a critical role in neurotransmitter exocytosis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. Publication Abstract from PubMed NSF (N-ethylmaleimide-sensitive factor) and alpha-SNAP (alpha-soluble NSF attachment protein) bind to the SNARE (soluble NSF attachment protein receptor) complex, the minimum machinery to mediate membrane fusion, to form a 20S complex, which disassembles the SNARE complex for reuse. We report the cryo-EM structures of the alpha-SNAP-SNARE subcomplex and the NSF-D1D2 domain in the 20S complex at 3.9- and 3.7-A resolutions, respectively. Combined with the biochemical and electrophysiological analyses, we find that alpha-SNAPs use R116 through electrostatic interactions and L197 through hydrophobic interactions to apply force mainly on two positions of the VAMP protein to execute disassembly process. Furthermore, we define the interaction between the amino terminus of the SNARE helical bundle and the pore loop of the NSF-D1 domain and demonstrate its essential role as a potential anchor for SNARE complex disassembly. Our studies provide a rotation model of alpha-SNAP-mediated disassembly of the SNARE complex. Mechanistic insights into the SNARE complex disassembly.,Huang X, Sun S, Wang X, Fan F, Zhou Q, Lu S, Cao Y, Wang QW, Dong MQ, Yao J, Sui SF Sci Adv. 2019 Apr 10;5(4):eaau8164. doi: 10.1126/sciadv.aau8164. eCollection 2019, Apr. PMID:30989110 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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