2cm5

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{{Seed}}
 
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[[Image:2cm5.png|left|200px]]
 
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==crystal structure of the C2B domain of rabphilin==
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The line below this paragraph, containing "STRUCTURE_2cm5", creates the "Structure Box" on the page.
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<StructureSection load='2cm5' size='340' side='right'caption='[[2cm5]], [[Resolution|resolution]] 1.28&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2cm5]] is a 1 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=2CM5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CM5 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.28&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_2cm5| PDB=2cm5 | SCENE= }}
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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=2cm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cm5 OCA], [https://pdbe.org/2cm5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cm5 RCSB], [https://www.ebi.ac.uk/pdbsum/2cm5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cm5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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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/cm/2cm5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2cm5 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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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.
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===CRYSTAL STRUCTURE OF THE C2B DOMAIN OF RABPHILIN===
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2cm5" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17166855}}, adds the Publication Abstract to the page
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*[[Exophilin 3D structures|Exophilin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17166855 is the PubMed ID number.
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*[[Rabphilin|Rabphilin]]
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== References ==
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{{ABSTRACT_PUBMED_17166855}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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2CM5 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CM5 OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:17166855</ref><references group="xtra"/>
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Becker, S.]]
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[[Category: Becker S]]
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[[Category: Montaville, P.]]
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[[Category: Montaville P]]
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[[Category: Schlicker, C.]]
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[[Category: Schlicker C]]
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[[Category: Sheldrick, G M.]]
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[[Category: Sheldrick GM]]
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[[Category: C2 domain]]
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[[Category: C2a-c2b linker fragment]]
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[[Category: C2b]]
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[[Category: Ca2+ binding]]
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[[Category: Metal-binding]]
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[[Category: Protein transport]]
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[[Category: Rabphilin3a]]
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[[Category: Synapse]]
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[[Category: Synaptic exocytosis]]
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[[Category: Transport]]
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[[Category: Zinc]]
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[[Category: Zinc-finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 10:35:10 2009''
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Current revision

crystal structure of the C2B domain of rabphilin

PDB ID 2cm5

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