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2cm6
From Proteopedia
(Difference between revisions)
(New page: 200px<br /> <applet load="2cm6" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cm6, resolution 1.85Å" /> '''CRYSTAL STRUCTURE O...) |
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| - | [[Image:2cm6.gif|left|200px]]<br /> | ||
| - | <applet load="2cm6" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2cm6, resolution 1.85Å" /> | ||
| - | '''CRYSTAL STRUCTURE OF THE C2B DOMAIN OF RABPHILIN3A'''<br /> | ||
| - | == | + | ==crystal structure of the C2B domain of rabphilin3A== |
| - | The Ca(2+) binding properties of C2 domains are essential for the function | + | <StructureSection load='2cm6' size='340' side='right'caption='[[2cm6]], [[Resolution|resolution]] 1.85Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2cm6]] is a 2 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=2CM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CM6 FirstGlance]. <br> | ||
| + | </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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=2cm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cm6 OCA], [https://pdbe.org/2cm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cm6 RCSB], [https://www.ebi.ac.uk/pdbsum/2cm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cm6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RP3A_RAT RP3A_RAT] Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cm/2cm6_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2cm6 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Ca(2+) binding properties of C2 domains are essential for the function of their host proteins. We present here the first crystal structures showing an unexpected Ca(2+) binding mode of the C2B domain of rabphilin-3A in atomic detail. Acidic residues from the linker region between the C2A and C2B domains of rabphilin-3A interact with the Ca(2+)-binding region of the C2B domain. Because of these interactions, the coordination sphere of the two bound Ca(2+) ions is almost complete. Mutation of these acidic residues to alanine resulted in a 10-fold decrease in the intrinsic Ca(2+) binding affinity of the C2B domain. Using NMR spectroscopy, we show that this interaction occurred only in the Ca(2+)-bound state of the C2B domain. In addition, this Ca(2+) binding mode was maintained in the C2 domain tandem fragment. In NMR-based liposome binding assays, the linker was not released upon phospholipid binding. Therefore, this unprecedented Ca(2+) binding mode not only shows how a C2 domain increases its intrinsic Ca(2+) affinity, but also provides the structural base for an atypical protein-Ca(2+)-phospholipid binding mode of rabphilin-3A. | ||
| - | + | The C2A-C2B linker defines the high affinity Ca(2+) binding mode of rabphilin-3A.,Montaville P, Schlicker C, Leonov A, Zweckstetter M, Sheldrick GM, Becker S J Biol Chem. 2007 Feb 16;282(7):5015-25. Epub 2006 Dec 13. PMID:17166855<ref>PMID:17166855</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2cm6" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Exophilin 3D structures|Exophilin 3D structures]] | ||
| + | *[[Rabphilin|Rabphilin]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rattus norvegicus]] | ||
| + | [[Category: Becker S]] | ||
| + | [[Category: Montaville P]] | ||
| + | [[Category: Schlicker C]] | ||
| + | [[Category: Sheldrick GM]] | ||
Current revision
crystal structure of the C2B domain of rabphilin3A
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