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[[Image:1t5t.gif|left|200px]]
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{{STRUCTURE_1t5t|  PDB=1t5t  |  SCENE=  }}
'''Structure of the (SR)Ca2+-ATPase Ca2-E1-ADP:AlF4- form'''


==Structure of the (SR)Ca2+-ATPase Ca2-E1-ADP:AlF4- form==
<StructureSection load='1t5t' size='340' side='right'caption='[[1t5t]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1t5t]] 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=1T5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T5T 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]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1t5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t5t OCA], [https://pdbe.org/1t5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t5t RCSB], [https://www.ebi.ac.uk/pdbsum/1t5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t5t 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/t5/1t5t_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=1t5t ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A tight coupling between adenosine triphosphate (ATP) hydrolysis and vectorial ion transport has to be maintained by ATP-consuming ion pumps. We report two crystal structures of Ca2+-bound sarco(endo)plasmic reticulum Ca2+-adenosine triphosphatase (SERCA) at 2.6 and 2.9 angstrom resolution in complex with (i) a nonhydrolyzable ATP analog [adenosine (beta-gamma methylene)-triphosphate] and (ii) adenosine diphosphate plus aluminum fluoride. SERCA reacts with ATP by an associative mechanism mediated by two Mg2+ ions to form an aspartyl-phosphorylated intermediate state (Ca2-E1 approximately P). The conformational changes that accompany the reaction with ATP pull the transmembrane helices 1 and 2 and close a cytosolic entrance for Ca2+, thereby preventing backflow before Ca2+ is released on the other side of the membrane.


==Overview==
Phosphoryl transfer and calcium ion occlusion in the calcium pump.,Sorensen TL, Moller JV, Nissen P Science. 2004 Jun 11;304(5677):1672-5. PMID:15192230<ref>PMID:15192230</ref>
A tight coupling between adenosine triphosphate (ATP) hydrolysis and vectorial ion transport has to be maintained by ATP-consuming ion pumps. We report two crystal structures of Ca2+-bound sarco(endo)plasmic reticulum Ca2+-adenosine triphosphatase (SERCA) at 2.6 and 2.9 angstrom resolution in complex with (i) a nonhydrolyzable ATP analog [adenosine (beta-gamma methylene)-triphosphate] and (ii) adenosine diphosphate plus aluminum fluoride. SERCA reacts with ATP by an associative mechanism mediated by two Mg2+ ions to form an aspartyl-phosphorylated intermediate state (Ca2-E1 approximately P). The conformational changes that accompany the reaction with ATP pull the transmembrane helices 1 and 2 and close a cytosolic entrance for Ca2+, thereby preventing backflow before Ca2+ is released on the other side of the membrane.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1T5T 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=1T5T OCA].
</div>
<div class="pdbe-citations 1t5t" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Phosphoryl transfer and calcium ion occlusion in the calcium pump., Sorensen TL, Moller JV, Nissen P, Science. 2004 Jun 11;304(5677):1672-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15192230 15192230]
*[[ATPase 3D structures|ATPase 3D structures]]
[[Category: Calcium-transporting ATPase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Single protein]]
[[Category: Moller JV]]
[[Category: Moller, J V.]]
[[Category: Nissen P]]
[[Category: Nissen, P.]]
[[Category: Sorensen TL-M]]
[[Category: Sorensen, T L.M.]]
[[Category: Calcium pump]]
[[Category: Catalytic mechanism]]
[[Category: Membrane protein]]
[[Category: Occlusion]]
[[Category: Phosphorylation]]
[[Category: Transition state]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:33:46 2008''

Latest revision as of 07:12, 13 August 2026

Structure of the (SR)Ca2+-ATPase Ca2-E1-ADP:AlF4- form

1t5t, resolution 2.90Å

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