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| | ==Crystal structure of the primed SNARE-Complexin-Synaptotagmin-1 C2AB complex== | | ==Crystal structure of the primed SNARE-Complexin-Synaptotagmin-1 C2AB complex== |
| - | <StructureSection load='5w5c' size='340' side='right' caption='[[5w5c]], [[Resolution|resolution]] 1.85Å' scene=''> | + | <StructureSection load='5w5c' size='340' side='right'caption='[[5w5c]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5w5c]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W5C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W5C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5w5c]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W5C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Vamp2, Syb2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Stx1a, Sap ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Snap25, Snap ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Cplx1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Syt1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5w5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w5c OCA], [http://pdbe.org/5w5c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w5c RCSB], [http://www.ebi.ac.uk/pdbsum/5w5c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w5c ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5w5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w5c OCA], [https://pdbe.org/5w5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w5c RCSB], [https://www.ebi.ac.uk/pdbsum/5w5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w5c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SYT1_RAT SYT1_RAT]] May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2. [[http://www.uniprot.org/uniprot/SNP25_RAT 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. [[http://www.uniprot.org/uniprot/VAMP2_RAT VAMP2_RAT]] Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). [[http://www.uniprot.org/uniprot/STX1A_RAT 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. [[http://www.uniprot.org/uniprot/CPLX1_RAT CPLX1_RAT]] Positively regulates a late step in synaptic vesicle exocytosis. Organizes the SNAREs into a cross-linked zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion, thereby preventing SNAREs from releasing neurotransmitters until an action potential arrives at the synapse. Also involved in glucose-induced secretion of insulin by pancreatic beta-cells (By similarity). | + | [https://www.uniprot.org/uniprot/VAMP2_RAT VAMP2_RAT] Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5w5c" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5w5c" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Complexin|Complexin]] |
| | + | *[[Synaptosomal-associated protein|Synaptosomal-associated protein]] |
| | + | *[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]] |
| | + | *[[Syntaxin 3D structures|Syntaxin 3D structures]] |
| | + | *[[Vesicle-associated membrane protein|Vesicle-associated membrane protein]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Large Structures]] |
| - | [[Category: Brunger, A T]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Zhou, Q]] | + | [[Category: Brunger AT]] |
| - | [[Category: Complexin]] | + | [[Category: Zhou Q]] |
| - | [[Category: Exocytosis]]
| + | |
| - | [[Category: Neuronal exocytosis]]
| + | |
| - | [[Category: Prefusion primed complex]]
| + | |
| - | [[Category: Snare complex]]
| + | |
| - | [[Category: Synaptotagmin]]
| + | |
| - | [[Category: Synchronous neurotransmitter release]]
| + | |
| Structural highlights
Function
VAMP2_RAT Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity).
Publication Abstract from PubMed
Synaptotagmin, complexin, and neuronal SNARE (soluble N-ethylmaleimide sensitive factor attachment protein receptor) proteins mediate evoked synchronous neurotransmitter release, but the molecular mechanisms mediating the cooperation between these molecules remain unclear. Here we determine crystal structures of the primed pre-fusion SNARE-complexin-synaptotagmin-1 complex. These structures reveal an unexpected tripartite interface between synaptotagmin-1 and both the SNARE complex and complexin. Simultaneously, a second synaptotagmin-1 molecule interacts with the other side of the SNARE complex via the previously identified primary interface. Mutations that disrupt either interface in solution also severely impair evoked synchronous release in neurons, suggesting that both interfaces are essential for the primed pre-fusion state. Ca2+ binding to the synaptotagmin-1 molecules unlocks the complex, allows full zippering of the SNARE complex, and triggers membrane fusion. The tripartite SNARE-complexin-synaptotagmin-1 complex at a synaptic vesicle docking site has to be unlocked for triggered fusion to start, explaining the cooperation between complexin and synaptotagmin-1 in synchronizing evoked release on the sub-millisecond timescale.
The primed SNARE-complexin-synaptotagmin complex for neuronal exocytosis.,Zhou Q, Zhou P, Wang AL, Wu D, Zhao M, Sudhof TC, Brunger AT Nature. 2017 Aug 24;548(7668):420-425. doi: 10.1038/nature23484. Epub 2017 Aug, 16. PMID:28813412[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhou Q, Zhou P, Wang AL, Wu D, Zhao M, Sudhof TC, Brunger AT. The primed SNARE-complexin-synaptotagmin complex for neuronal exocytosis. Nature. 2017 Aug 24;548(7668):420-425. doi: 10.1038/nature23484. Epub 2017 Aug, 16. PMID:28813412 doi:http://dx.doi.org/10.1038/nature23484
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