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2c88

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(New page: 200px<br /> <applet load="2c88" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c88, resolution 3.10&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:2c88.gif|left|200px]]<br />
 
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<applet load="2c88" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2c88, resolution 3.10&Aring;" />
 
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'''CRYSTAL STRUCTURE OF (SR) CALCIUM-ATPASE E2(TG):AMPPCP FORM'''<br />
 
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==Overview==
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==Crystal Structure Of (SR) Calcium-ATPase E2(Tg):AMPPCP form==
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We present crystal structures of the calcium-free E2 state of the, sarcoplasmic reticulum Ca2+ -ATPase, stabilized by the inhibitor, thapsigargin and the ATP analog AMPPCP. The structures allow us to, describe the ATP binding site in a modulatory mode uncoupled from the, Asp351 phosphorylation site. The Glu439 side chain interacts with AMPPCP, via an Mg2+ ion in accordance with previous Fe2+ -cleavage studies, implicating this residue in the ATPase cycle and in magnesium binding., Functional data on Ca2+ mediated activation indicate that the crystallized, state represents an initial stage of ATP modulated deprotonation of E2, preceding the binding of Ca2+ ions in the membrane from the cytoplasmic, side. We propose a mechanism of Ca2+ activation of phosphorylation leading, directly from ... [[http://ispc.weizmann.ac.il/pmbin/getpm?16710301 (full description)]]
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<StructureSection load='2c88' size='340' side='right'caption='[[2c88]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2c88]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C88 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]] 3.1&#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=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TG1:OCTANOIC+ACID+[3S-[3ALPHA,+3ABETA,+4ALPHA,+6BETA,+6ABETA,+7BETA,+8ALPHA(Z),+9BALPHA]]-6-(ACETYLOXY)-2,3,-3A,4,5,6,6A,7,8,9B-DECAHYDRO-3,3A-DIHYDROXY-3,6,9-TRIMETHYL-8-[(2-METHYL-1-OXO-2-BUTENYL)OX+Y]-2-OXO-4-(1-OXOBUTOXY)-AZULENO[4,5-B]FURAN-7-YL+ESTER'>TG1</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=2c88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c88 OCA], [https://pdbe.org/2c88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c88 RCSB], [https://www.ebi.ac.uk/pdbsum/2c88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c88 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AT2A1_RABIT AT2A1_RABIT] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity).
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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/c8/2c88_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=2c88 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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We present crystal structures of the calcium-free E2 state of the sarcoplasmic reticulum Ca2+ -ATPase, stabilized by the inhibitor thapsigargin and the ATP analog AMPPCP. The structures allow us to describe the ATP binding site in a modulatory mode uncoupled from the Asp351 phosphorylation site. The Glu439 side chain interacts with AMPPCP via an Mg2+ ion in accordance with previous Fe2+ -cleavage studies implicating this residue in the ATPase cycle and in magnesium binding. Functional data on Ca2+ mediated activation indicate that the crystallized state represents an initial stage of ATP modulated deprotonation of E2, preceding the binding of Ca2+ ions in the membrane from the cytoplasmic side. We propose a mechanism of Ca2+ activation of phosphorylation leading directly from the compact E2-ATP form to the Ca2E1-ATP state. In addition, a role of Glu439 in ATP modulation of other steps of the functional cycle is suggested.
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==About this Structure==
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Modulatory and catalytic modes of ATP binding by the calcium pump.,Jensen AM, Sorensen TL, Olesen C, Moller JV, Nissen P EMBO J. 2006 Jun 7;25(11):2305-14. Epub 2006 May 18. PMID:16710301<ref>PMID:16710301</ref>
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2C88 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]] with MG, NA, TG1 and ACP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C88 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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Modulatory and catalytic modes of ATP binding by the calcium pump., Jensen AM, Sorensen TL, Olesen C, Moller JV, Nissen P, EMBO J. 2006 Jun 7;25(11):2305-14. Epub 2006 May 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16710301 16710301]
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</div>
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[[Category: Oryctolagus cuniculus]]
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<div class="pdbe-citations 2c88" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Jensen, A.M.]]
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[[Category: Moller, J.V.]]
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[[Category: Nissen, P.]]
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[[Category: Olesen, C.]]
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[[Category: Sorensen, T.L.]]
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[[Category: ACP]]
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[[Category: MG]]
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[[Category: NA]]
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[[Category: TG1]]
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[[Category: ca2+]]
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[[Category: ca2+-atpase]]
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[[Category: cation pump]]
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[[Category: hydrolase]]
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[[Category: ion transport]]
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[[Category: magnesium]]
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[[Category: membrane protein]]
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[[Category: metal-binding]]
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[[Category: modulatory atp]]
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[[Category: nucleotide-binding]]
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[[Category: p-type atpase]]
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[[Category: phosphorylation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:55:03 2007''
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==See Also==
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*[[ATPase 3D structures|ATPase 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: Large Structures]]
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[[Category: Oryctolagus cuniculus]]
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[[Category: Jensen AM]]
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[[Category: Moller JV]]
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[[Category: Nissen P]]
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[[Category: Olesen C]]
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[[Category: Sorensen TL]]

Current revision

Crystal Structure Of (SR) Calcium-ATPase E2(Tg):AMPPCP form

PDB ID 2c88

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