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| | ==Synaptotagmin-7, C2B-domain, calcium bound== | | ==Synaptotagmin-7, C2B-domain, calcium bound== |
| - | <StructureSection load='3n5a' size='340' side='right' caption='[[3n5a]], [[Resolution|resolution]] 1.44Å' scene=''> | + | <StructureSection load='3n5a' size='340' side='right'caption='[[3n5a]], [[Resolution|resolution]] 1.44Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3n5a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N5A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N5A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3n5a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N5A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 1.441Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Syt7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=3n5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n5a OCA], [http://pdbe.org/3n5a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n5a RCSB], [http://www.ebi.ac.uk/pdbsum/3n5a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n5a 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=3n5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n5a OCA], [https://pdbe.org/3n5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n5a RCSB], [https://www.ebi.ac.uk/pdbsum/3n5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n5a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SYT7_MOUSE SYT7_MOUSE]] May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). | + | [https://www.uniprot.org/uniprot/SYT7_MOUSE SYT7_MOUSE] May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Synaptotagmin|Synaptotagmin]] | + | *[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Craig, T K]] | + | [[Category: Mus musculus]] |
| - | [[Category: Rizo, J]] | + | [[Category: Craig TK]] |
| - | [[Category: Tomchick, D R]] | + | [[Category: Rizo J]] |
| - | [[Category: Calcium/phospholipid binding protein]] | + | [[Category: Tomchick DR]] |
| - | [[Category: Protein transport]]
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| Structural highlights
Function
SYT7_MOUSE May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Synaptotagmins are known to mediate diverse forms of Ca2+-triggered exocytosis through their C2 domains, but the principles underlying functional differentiation among them are unclear. Synaptotagmin-1 functions as a Ca2+ sensor in neurotransmitter release at central nervous system synapses, but synaptotagmin-7 does not, and yet both isoforms act as Ca2+ sensors in chromaffin cells. To shed light into this apparent paradox, we have performed rescue experiments in neurons from synaptotagmin-1 knockout mice using a chimera that contains the synaptotagmin-1 sequence with its C2B domain replaced by the synaptotagmin-7 C2B domain (Syt1/7). Rescue was not achieved either with the WT Syt1/7 chimera or with nine mutants where residues that are distinct in synaptotagmin-7 were restored to those present in synaptotagmin-1. To investigate whether these results arise because of unique conformational features of the synaptotagmin-7 C2B domain, we determined its crystal structure at 1.44 A resolution. The synaptotagmin-7 C2B domain structure is very similar to that of the synaptotagmin-1 C2B domain and contains three Ca2+-binding sites. Two of the Ca2+-binding sites of the synaptotagmin-7 C2B domain are also present in the synaptotagmin-1 C2B domain and have analogous ligands to those determined for the latter by NMR spectroscopy, suggesting that a discrepancy observed in a crystal structure of the synaptotagmin-1 C2B domain arose from crystal contacts. Overall, our results suggest that functional differentiation in synaptotagmins arises in part from subtle sequence changes that yield dramatic functional differences.
Structural and mutational analysis of functional differentiation between synaptotagmins-1 and -7.,Xue M, Craig TK, Shin OH, Li L, Brautigam CA, Tomchick DR, Sudhof TC, Rosenmund C, Rizo J PLoS One. 2010 Sep 2;5(9). pii: e12544. PMID:20824061[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Xue M, Craig TK, Shin OH, Li L, Brautigam CA, Tomchick DR, Sudhof TC, Rosenmund C, Rizo J. Structural and mutational analysis of functional differentiation between synaptotagmins-1 and -7. PLoS One. 2010 Sep 2;5(9). pii: e12544. PMID:20824061 doi:10.1371/journal.pone.0012544
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