|
|
| Line 3: |
Line 3: |
| | <SX load='6mti' size='340' side='right' viewer='molstar' caption='[[6mti]], [[Resolution|resolution]] 10.40Å' scene=''> | | <SX load='6mti' size='340' side='right' viewer='molstar' caption='[[6mti]], [[Resolution|resolution]] 10.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6mti]] is a 30 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=6MTI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6MTI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mti]] is a 30 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=6MTI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MTI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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">Electron Microscopy, [[Resolution|Resolution]] 10.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Syt1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), 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])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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://proteopedia.org/fgij/fg.htm?mol=6mti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mti OCA], [http://pdbe.org/6mti PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mti RCSB], [http://www.ebi.ac.uk/pdbsum/6mti PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mti 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=6mti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mti OCA], [https://pdbe.org/6mti PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mti RCSB], [https://www.ebi.ac.uk/pdbsum/6mti PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mti ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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/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/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/VAMP2_RAT VAMP2_RAT]] Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). | + | [https://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. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Synapotagmin-1 (Syt1) interacts with both SNARE proteins and lipid membranes to synchronize neurotransmitter release to calcium (Ca(2+)) influx. Here we report the cryo-electron microscopy structure of the Syt1-SNARE complex on anionic-lipid containing membranes. Under resting conditions, the Syt1 C2 domains bind the membrane with a magnesium (Mg(2+))-mediated partial insertion of the aliphatic loops, alongside weak interactions with the anionic lipid headgroups. The C2B domain concurrently interacts the SNARE bundle via the 'primary' interface and is positioned between the SNAREpins and the membrane. In this configuration, Syt1 is projected to sterically delay the complete assembly of the associated SNAREpins and thus, contribute to clamping fusion. This Syt1-SNARE organization is disrupted upon Ca(2+)-influx as Syt1 reorients into the membrane, likely displacing the attached SNAREpins and reversing the fusion clamp. We thus conclude that the cation (Mg(2+)/Ca(2+)) dependent membrane interaction is a key determinant of the dual clamp/activator function of Synaptotagmin-1.
| + | |
| - | | + | |
| - | Structural basis for the clamping and Ca(2+) activation of SNARE-mediated fusion by synaptotagmin.,Grushin K, Wang J, Coleman J, Rothman JE, Sindelar CV, Krishnakumar SS Nat Commun. 2019 Jun 3;10(1):2413. doi: 10.1038/s41467-019-10391-x. PMID:31160571<ref>PMID:31160571</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6mti" style="background-color:#fffaf0;"></div>
| + | |
| | | | |
| | ==See Also== | | ==See Also== |
| | *[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]] | | *[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]] |
| | *[[Syntaxin 3D structures|Syntaxin 3D structures]] | | *[[Syntaxin 3D structures|Syntaxin 3D structures]] |
| - | == References ==
| + | *[[Vesicle-associated membrane protein|Vesicle-associated membrane protein]] |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Coleman, J]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Grushin, K]] | + | [[Category: Coleman J]] |
| - | [[Category: Krishnakumar, S]] | + | [[Category: Grushin K]] |
| - | [[Category: Rothman, J]] | + | [[Category: Krishnakumar S]] |
| - | [[Category: Sindelar, C]] | + | [[Category: Rothman J]] |
| - | [[Category: Wang, J]] | + | [[Category: Sindelar C]] |
| - | [[Category: Exocytosis]]
| + | [[Category: Wang J]] |
| - | [[Category: Lipid nanotube]]
| + | |
| - | [[Category: Snare]]
| + | |
