5h4y: Difference between revisions

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<StructureSection load='5h4y' size='340' side='right'caption='[[5h4y]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='5h4y' size='340' side='right'caption='[[5h4y]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5h4y]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H4Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5H4Y FirstGlance]. <br>
<table><tr><td colspan='2'>[[5h4y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H4Y FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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]] 1.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h4z|5h4z]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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://proteopedia.org/fgij/fg.htm?mol=5h4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h4y OCA], [http://pdbe.org/5h4y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h4y RCSB], [http://www.ebi.ac.uk/pdbsum/5h4y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h4y 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=5h4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h4y OCA], [https://pdbe.org/5h4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h4y RCSB], [https://www.ebi.ac.uk/pdbsum/5h4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h4y ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SYT5_HUMAN SYT5_HUMAN]] 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. Regulates the Ca(2+)-dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface (By similarity).  
[https://www.uniprot.org/uniprot/SYT5_HUMAN SYT5_HUMAN] 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. Regulates the Ca(2+)-dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Synaptotagmins constitute a family of multifunctional integral membrane proteins found predominantly on vesicles in neural and endocrine tissues. 17 isoforms of synaptotagmin family in mammals have been identified, 7 isoforms among them are known to be able to bind Ca2+ via their C2 domains. This study presents the crystal structure of the first C2 domain (C2A domain) of synaptotagmin 5 complexed with Ca2+ at 1.90A resolution. Comparison of the Ca2+-binding pocket of synaptotagmin 5 C2A domain with other synaptotagmin C2 domains demonstrated that a serine residue locating at Ca2+-binding loop probably responsible to the conformational variation of Ca2+-binding pocket, and thus impacts the Ca2+-binding mechanism of C2 domain, which is verified by structural analysis of the serine mutant and Ca2+-binding assays via isothermal titration calorimetry. Alteration of Ca2+-binding mechanism might be correlated with different Ca2+ response rates of synaptotagmins, which is the basis of the functions of synaptotagmins in regulating various types of Ca2+-triggered vesicle-membrane fusion processes.
 
Structural analysis of Ca2+-binding pocket of synaptotagmin 5 C2A domain.,Qiu X, Ge J, Gao Y, Teng M, Niu L Int J Biol Macromol. 2016 Oct 25. pii: S0141-8130(16)32153-5. doi:, 10.1016/j.ijbiomac.2016.10.083. PMID:27793683<ref>PMID:27793683</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5h4y" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]]
*[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gao, Y]]
[[Category: Gao Y]]
[[Category: Niu, L]]
[[Category: Niu L]]
[[Category: Qiu, X]]
[[Category: Qiu X]]
[[Category: Teng, M]]
[[Category: Teng M]]
[[Category: Metal binding protein]]
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