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3ba6

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[[Image:3ba6.png|left|200px]]
 
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{{STRUCTURE_3ba6| PDB=3ba6 | SCENE= }}
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==Structure of the Ca2E1P phosphoenzyme intermediate of the SERCA Ca2+-ATPase==
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<StructureSection load='3ba6' size='340' side='right'caption='[[3ba6]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3ba6]] 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=3BA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BA6 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]] 2.8&#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=AN2:AMP+PHOSPHORAMIDATE'>AN2</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</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=3ba6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ba6 OCA], [https://pdbe.org/3ba6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ba6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ba6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ba6 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/ba/3ba6_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=3ba6 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 sarcoplasmic reticulum Ca2+-ATPase, a P-type ATPase, has a critical role in muscle function and metabolism. Here we present functional studies and three new crystal structures of the rabbit skeletal muscle Ca2+-ATPase, representing the phosphoenzyme intermediates associated with Ca2+ binding, Ca2+ translocation and dephosphorylation, that are based on complexes with a functional ATP analogue, beryllium fluoride and aluminium fluoride, respectively. The structures complete the cycle of nucleotide binding and cation transport of Ca2+-ATPase. Phosphorylation of the enzyme triggers the onset of a conformational change that leads to the opening of a luminal exit pathway defined by the transmembrane segments M1 through M6, which represent the canonical membrane domain of P-type pumps. Ca2+ release is promoted by translocation of the M4 helix, exposing Glu 309, Glu 771 and Asn 796 to the lumen. The mechanism explains how P-type ATPases are able to form the steep electrochemical gradients required for key functions in eukaryotic cells.
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===Structure of the Ca2E1P phosphoenzyme intermediate of the SERCA Ca2+-ATPase===
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The structural basis of calcium transport by the calcium pump.,Olesen C, Picard M, Winther AM, Gyrup C, Morth JP, Oxvig C, Moller JV, Nissen P Nature. 2007 Dec 13;450(7172):1036-42. PMID:18075584<ref>PMID:18075584</ref>
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{{ABSTRACT_PUBMED_18075584}}
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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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==About this Structure==
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<div class="pdbe-citations 3ba6" style="background-color:#fffaf0;"></div>
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[[3ba6]] is a 1 chain structure of [[ATPase]] with 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=3BA6 OCA].
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==See Also==
==See Also==
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*[[ATPase|ATPase]]
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*[[ATPase 3D structures|ATPase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:018075584</ref><ref group="xtra">PMID:018956892</ref><references group="xtra"/>
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__TOC__
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[[Category: Calcium-transporting ATPase]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Gyrup, C.]]
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[[Category: Gyrup C]]
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[[Category: Moller, J V.]]
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[[Category: Moller JV]]
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[[Category: Morth, J P.]]
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[[Category: Morth JP]]
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[[Category: Nissen, P.]]
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[[Category: Nissen P]]
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[[Category: Olesen, C.]]
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[[Category: Olesen C]]
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[[Category: Oxvig, C.]]
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[[Category: Oxvig C]]
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[[Category: Picard, M.]]
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[[Category: Picard M]]
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[[Category: Winther, A M.L.]]
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[[Category: Winther AML]]
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[[Category: Aspartyl-phosphoanhydride]]
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[[Category: Atp-binding]]
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[[Category: Calcium transport]]
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[[Category: Endoplasmic reticulum]]
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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: Nucleotide-binding]]
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[[Category: P-type atpase]]
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[[Category: Phosphoenzyme]]
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[[Category: Phosphorylation]]
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[[Category: Sarcoplasmic reticulum]]
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[[Category: Transmembrane]]
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[[Category: Transport]]
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Current revision

Structure of the Ca2E1P phosphoenzyme intermediate of the SERCA Ca2+-ATPase

PDB ID 3ba6

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