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2r83

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(New page: 200px<br /><applet load="2r83" size="350" color="white" frame="true" align="right" spinBox="true" caption="2r83, resolution 2.70&Aring;" /> '''Crystal structure an...)
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[[Image:2r83.jpg|left|200px]]<br /><applet load="2r83" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2r83, resolution 2.70&Aring;" />
 
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'''Crystal structure analysis of human synaptotagmin 1 C2A-C2B'''<br />
 
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==Overview==
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==Crystal structure analysis of human synaptotagmin 1 C2A-C2B==
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Release of neurotransmitter from synaptic vesicles requires the, Ca2+/phospholipid-binding protein synaptotagmin 1. There is considerable, evidence that cooperation between the tandem C2 domains of synaptotagmin, is a requirement of regulated exocytosis; however, high-resolution, structural evidence for this interaction has been lacking. The 2.7 A, crystal structure of the cytosolic domains of human synaptotagmin 1 in the, absence of Ca2+ reveals a novel closed conformation of the protein. The, shared interface between C2A and C2B is stabilized by a network of, interactions between residues on the C-terminal alpha-helix of the C2B, domain and residues on loops 1-3 of the Ca2+-binding region of C2A. These, interactions alter the overall shape of the Ca2+-binding pocket of C2A, but not that of C2B. Thus, synaptotagmin 1 C2A-C2B may utilize a novel, regulatory mechanism whereby one C2 domain could regulate the other until, an appropriate triggering event decouples them.
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<StructureSection load='2r83' size='340' side='right'caption='[[2r83]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2r83]] is a 2 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=2R83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R83 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2r83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r83 OCA], [https://pdbe.org/2r83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r83 RCSB], [https://www.ebi.ac.uk/pdbsum/2r83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r83 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYT1_HUMAN SYT1_HUMAN] 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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r8/2r83_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2r83 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Release of neurotransmitter from synaptic vesicles requires the Ca2+/phospholipid-binding protein synaptotagmin 1. There is considerable evidence that cooperation between the tandem C2 domains of synaptotagmin is a requirement of regulated exocytosis; however, high-resolution structural evidence for this interaction has been lacking. The 2.7 A crystal structure of the cytosolic domains of human synaptotagmin 1 in the absence of Ca2+ reveals a novel closed conformation of the protein. The shared interface between C2A and C2B is stabilized by a network of interactions between residues on the C-terminal alpha-helix of the C2B domain and residues on loops 1-3 of the Ca2+-binding region of C2A. These interactions alter the overall shape of the Ca2+-binding pocket of C2A, but not that of C2B. Thus, synaptotagmin 1 C2A-C2B may utilize a novel regulatory mechanism whereby one C2 domain could regulate the other until an appropriate triggering event decouples them.
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==About this Structure==
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Structure of human synaptotagmin 1 C2AB in the absence of Ca2+ reveals a novel domain association.,Fuson KL, Montes M, Robert JJ, Sutton RB Biochemistry. 2007 Nov 13;46(45):13041-8. Epub 2007 Oct 23. PMID:17956130<ref>PMID:17956130</ref>
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2R83 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=AC1:Cl+Binding+Site+For+Residue+A+101'>AC1</scene>, <scene name='pdbsite=AC2:Cl+Binding+Site+For+Residue+A+102'>AC2</scene>, <scene name='pdbsite=AC3:Cl+Binding+Site+For+Residue+A+103'>AC3</scene>, <scene name='pdbsite=AC4:Cl+Binding+Site+For+Residue+A+104'>AC4</scene>, <scene name='pdbsite=AC5:Cl+Binding+Site+For+Residue+A+105'>AC5</scene>, <scene name='pdbsite=AC6:Cl+Binding+Site+For+Residue+B+106'>AC6</scene>, <scene name='pdbsite=AC7:Cl+Binding+Site+For+Residue+B+107'>AC7</scene> and <scene name='pdbsite=AC8:Cl+Binding+Site+For+Residue+A+108'>AC8</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R83 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of human synaptotagmin 1 C2AB in the absence of Ca2+ reveals a novel domain association., Fuson KL, Montes M, Robert JJ, Sutton RB, Biochemistry. 2007 Nov 13;46(45):13041-8. Epub 2007 Oct 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17956130 17956130]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 2r83" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Fuson, K.L]]
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[[Category: Montes, M.]]
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[[Category: Robert, J.J]]
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[[Category: Sutton, R.B.]]
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[[Category: CL]]
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[[Category: c2a-c2b]]
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[[Category: calcium]]
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[[Category: cell junction]]
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[[Category: cytoplasmic vesicle]]
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[[Category: endocytosis]]
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[[Category: endocytosis/exocytosis complex]]
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[[Category: exocytosis]]
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[[Category: glycoprotein]]
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[[Category: lipoprotein]]
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[[Category: membrane]]
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[[Category: metal-binding]]
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[[Category: palmitate]]
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[[Category: phosphorylation]]
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[[Category: synapse]]
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[[Category: transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:21:29 2008''
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==See Also==
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*[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Fuson KL]]
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[[Category: Montes M]]
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[[Category: Robert JJ]]
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[[Category: Sutton RB]]

Current revision

Crystal structure analysis of human synaptotagmin 1 C2A-C2B

PDB ID 2r83

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