2c8k: Difference between revisions

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-[[Image:2c8k.gif|left|200px]]
- {{Structure
+==Crystal Structure of (SR) Calcium-ATPase E2(Tg) with partially occupied AMPPCP site==
-|PDB= 2c8k |SIZE=350|CAPTION= <scene name='initialview01'>2c8k</scene>, resolution 2.80&Aring;
+<StructureSection load='2c8k' size='340' side='right'caption='[[2c8k]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-|SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene>
+== Structural highlights ==
-|LIGAND= <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)OXY]-2-OXO-4-(1-OXOBUTOXY)-AZULENO[4,5-B]FURAN-7-YL+ESTER'>TG1</scene>
+<table><tr><td colspan='2'>[[2c8k]] 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=2C8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C8K FirstGlance]. <br>
-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium-transporting_ATPase Calcium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8] </span>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-|GENE=
+<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>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c8k OCA], [https://pdbe.org/2c8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c8k RCSB], [https://www.ebi.ac.uk/pdbsum/2c8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c8k ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c8k OCA], [http://www.ebi.ac.uk/pdbsum/2c8k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c8k RCSB]</span>
+== Function ==
-}}
+[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).
+== 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/c8/2c8k_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=2c8k ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-'''CRYSTAL STRUCTURE OF (SR) CALCIUM-ATPASE E2(TG) WITH PARTIALLY OCCUPIED AMPPCP SITE'''
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2c8k" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[ATPase 3D structures|ATPase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-C8K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C8K OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-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://www.ncbi.nlm.nih.gov/pubmed/16710301 16710301]
-[[Category: Calcium-transporting ATPase]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Single protein]]
+[[Category: Jensen AM]]
-[[Category: Jensen, A M.]]
+[[Category: Moller JV]]
-[[Category: Moller, J V.]]
+[[Category: Nissen P]]
-[[Category: Nissen, P.]]
+[[Category: Olesen C]]
-[[Category: Olesen, C.]]
+[[Category: Sorensen TL]]
-[[Category: Sorensen, T L.]]
-[[Category: atp-binding]]
-[[Category: ca2+-atpase]]
-[[Category: calcium transport]]
-[[Category: cation pump]]
-[[Category: hydrolase]]
-[[Category: ion transport]]
-[[Category: membrane protein]]
-[[Category: metal-binding]]
-[[Category: modulatory atp]]
-[[Category: nucleotide-binding]]
-[[Category: p-type atpase]]
-[[Category: phosphorylation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:17:56 2008''