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New page: left|200px<br /><applet load="1vfp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vfp, resolution 2.90Å" /> '''Crystal structure of...
 
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[[Image:1vfp.jpg|left|200px]]<br /><applet load="1vfp" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1vfp, resolution 2.90&Aring;" />
'''Crystal structure of the SR CA2+-ATPase with bound AMPPCP'''<br />


==Overview==
==Crystal structure of the SR CA2+-ATPase with bound AMPPCP==
P-type ATPases are ATP-powered ion pumps that establish ion concentration, gradients across cell and organelle membranes. Here, we describe the, crystal structure of the Ca2+ pump of skeletal muscle sarcoplasmic, reticulum, a representative member of the P-type ATPase superfamily, with, an ATP analogue, a Mg2+ and two Ca2+ ions in the respective binding sites., In this state, the ATP analogue reorganizes the three cytoplasmic domains, (A, N and P), which are widely separated without nucleotide, by directly, bridging the N and P domains. The structure of the P-domain itself is, altered by the binding of the ATP analogue and Mg2+. As a result, the, A-domain is tilted so that one of the transmembrane helices moves to lock, the cytoplasmic gate of the transmembrane Ca2+-binding sites. This appears, to be the mechanism for occluding the bound Ca2+ ions, before releasing, them into the lumen of the sarcoplasmic reticulum.
<StructureSection load='1vfp' size='340' side='right'caption='[[1vfp]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1vfp]] is a 2 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=1VFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VFP 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=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1vfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vfp OCA], [https://pdbe.org/1vfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vfp RCSB], [https://www.ebi.ac.uk/pdbsum/1vfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vfp 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/vf/1vfp_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=1vfp ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
P-type ATPases are ATP-powered ion pumps that establish ion concentration gradients across cell and organelle membranes. Here, we describe the crystal structure of the Ca2+ pump of skeletal muscle sarcoplasmic reticulum, a representative member of the P-type ATPase superfamily, with an ATP analogue, a Mg2+ and two Ca2+ ions in the respective binding sites. In this state, the ATP analogue reorganizes the three cytoplasmic domains (A, N and P), which are widely separated without nucleotide, by directly bridging the N and P domains. The structure of the P-domain itself is altered by the binding of the ATP analogue and Mg2+. As a result, the A-domain is tilted so that one of the transmembrane helices moves to lock the cytoplasmic gate of the transmembrane Ca2+-binding sites. This appears to be the mechanism for occluding the bound Ca2+ ions, before releasing them into the lumen of the sarcoplasmic reticulum.


==About this Structure==
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:15229613<ref>PMID:15229613</ref>
1VFP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with CA, MG and ACP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VFP OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15229613 15229613]
</div>
[[Category: Calcium-transporting ATPase]]
<div class="pdbe-citations 1vfp" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Single protein]]
[[Category: Mizutani T]]
[[Category: Mizutani, T.]]
[[Category: Toyoshima C]]
[[Category: Toyoshima, C.]]
[[Category: ACP]]
[[Category: CA]]
[[Category: MG]]
[[Category: had fold]]
[[Category: membrane protein]]
[[Category: p-type atpase]]
 
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Retrieved from "https://proteopedia.org/1vfp"