2ear: Difference between revisions

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-{{Seed}}
-[[Image:2ear.png|left|200px]]
-<!--
+==P21 crystal of the SR CA2+-ATPase with bound TG==
-The line below this paragraph, containing "STRUCTURE_2ear", creates the "Structure Box" on the page.
+<StructureSection load='2ear' size='340' side='right'caption='[[2ear]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2ear]] 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=2EAR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EAR FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=TG1:[(3S,3aR,4S,6S,6aR,7S,8S,9bS)-6-acetyloxy-4-butanoyloxy-3,3a-dihydroxy-3,6,9-trimethyl-8-[(Z)-2-methylbut-2-enoyl]oxy-2-oxo-4,5,6a,7,8,9b-hexahydroazuleno[4,5-b]furan-7-yl]+octanoate'>TG1</scene></td></tr>
-{{STRUCTURE_2ear|  PDB=2ear  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ear FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ear OCA], [https://pdbe.org/2ear PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ear RCSB], [https://www.ebi.ac.uk/pdbsum/2ear PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ear ProSAT]</span></td></tr>
+</table>
+== 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/ea/2ear_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2ear ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Ca(2+)-ATPase of skeletal muscle sarcoplasmic reticulum is an ATP-driven Ca(2+) pump consisting of three cytoplasmic domains and 10 transmembrane helices. In the absence of Ca(2+), the three cytoplasmic domains gather to form a compact headpiece, but the ATPase is unstable without an inhibitor. Here we describe the crystal structures of Ca(2+)-ATPase in the absence of Ca(2+) stabilized with cyclopiazonic acid alone and in combination with other inhibitors. Cyclopiazonic acid is located in the transmembrane region of the protein near the cytoplasmic surface. The binding site partially overlaps with that of 2,5-di-tert-butyl-1,4-dihydroxybenzene but is separate from that of thapsigargin. The overall structure is significantly different from that stabilized with thapsigargin: The cytoplasmic headpiece is more upright, and the transmembrane helices M1-M4 are rearranged. Cyclopiazonic acid primarily alters the position of the M1' helix and thereby M2 and M4 and then M5. Because M5 is integrated into the phosphorylation domain, the whole cytoplasmic headpiece moves. These structural changes show how an event in the transmembrane domain can be transmitted to the cytoplasmic domain despite flexible links between them. They also reveal that Ca(2+)-ATPase has considerable plasticity even when fixed by a transmembrane inhibitor, presumably to accommodate thermal fluctuations.
-===P21 crystal of the SR CA2+-ATPase with bound TG===
+Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors.,Takahashi M, Kondou Y, Toyoshima C Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5800-5. Epub 2007 Mar 26. PMID:17389383<ref>PMID:17389383</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2ear" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17389383}}, adds the Publication Abstract to the page
+*[[ATPase 3D structures|ATPase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17389383 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17389383}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-EAR 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=2EAR OCA].
-==Reference==
-Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors., Takahashi M, Kondou Y, Toyoshima C, Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5800-5. Epub 2007 Mar 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17389383 17389383]
-Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution., Toyoshima C, Nakasako M, Nomura H, Ogawa H, Nature. 2000 Jun 8;405(6787):647-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10864315 10864315]
-Structural changes in the calcium pump accompanying the dissociation of calcium., Toyoshima C, Nomura H, Nature. 2002 Aug 8;418(6898):605-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12167852 12167852]
-Crystal structure of the calcium pump with a bound ATP analogue., Toyoshima C, Mizutani T, Nature. 2004 Jul 29;430(6999):529-35. Epub 2004 Jun 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15229613 15229613]
-Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues., Toyoshima C, Nomura H, Tsuda T, Nature. 2004 Nov 18;432(7015):361-8. Epub 2004 Sep 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15448704 15448704]
-Structural role of countertransport revealed in Ca(2+) pump crystal structure in the absence of Ca(2+)., Obara K, Miyashita N, Xu C, Toyoshima I, Sugita Y, Inesi G, Toyoshima C, Proc Natl Acad Sci U S A. 2005 Oct 11;102(41):14489-96. Epub 2005 Sep 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16150713 16150713]
-[[Category: Calcium-transporting ATPase]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Single protein]]
+[[Category: Kondou Y]]
-[[Category: Kondou, Y.]]
+[[Category: Takahashi M]]
-[[Category: Takahashi, M.]]
+[[Category: Toyoshima C]]
-[[Category: Toyoshima, C.]]
-[[Category: Ca2+]]
-[[Category: Had fold]]
-[[Category: Hydrolase]]
-[[Category: Ion pump]]
-[[Category: Membrane protein]]
-[[Category: P-type atpase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:40:51 2008''