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[[Image:3b9b.png|left|200px]]


{{STRUCTURE_3b9b| PDB=3b9b | SCENE= }}
==Structure of the E2 beryllium fluoride complex of the SERCA Ca2+-ATPase==
<StructureSection load='3b9b' size='340' side='right'caption='[[3b9b]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3b9b]] 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=3B9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B9B FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b9b OCA], [https://pdbe.org/3b9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b9b RCSB], [https://www.ebi.ac.uk/pdbsum/3b9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b9b 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/b9/3b9b_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=3b9b ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


===Structure of the E2 beryllium fluoride complex of the SERCA Ca2+-ATPase===
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>


{{ABSTRACT_PUBMED_18075584}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 3b9b" style="background-color:#fffaf0;"></div>
[[3b9b]] 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=3B9B OCA].


==See Also==
==See Also==
*[[ATPase|ATPase]]
*[[ATPase 3D structures|ATPase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:018075584</ref><ref group="xtra">PMID:018956892</ref><references group="xtra"/>
__TOC__
[[Category: Calcium-transporting ATPase]]
</StructureSection>
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Moller, J V.]]
[[Category: Moller JV]]
[[Category: Morth, J P.]]
[[Category: Morth JP]]
[[Category: Nissen, P.]]
[[Category: Nissen P]]
[[Category: Olesen, C.]]
[[Category: Olesen C]]
[[Category: Picard, M.]]
[[Category: Picard M]]
[[Category: Winther, A M.L.]]
[[Category: Winther AML]]
[[Category: Atp-binding]]
[[Category: Beryllium fluoride]]
[[Category: Ca2+-atpase]]
[[Category: Calcium transport]]
[[Category: Endoplasmic reticulum]]
[[Category: Hydrolase]]
[[Category: Ion transport]]
[[Category: Magnesium]]
[[Category: Membrane protein]]
[[Category: Metal-binding]]
[[Category: Nucleotide-binding]]
[[Category: P-type atpase]]
[[Category: Phosphorylation]]
[[Category: Sarcoplasmic reticulum]]
[[Category: Transmembrane]]
[[Category: Transport]]
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