1wpg

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[[Image:1wpg.jpg|left|200px]]<br /><applet load="1wpg" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1wpg.jpg|left|200px]]
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caption="1wpg, resolution 2.30&Aring;" />
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'''Crystal structure of the SR CA2+-ATPase with MGF4'''<br />
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{{Structure
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|PDB= 1wpg |SIZE=350|CAPTION= <scene name='initialview01'>1wpg</scene>, resolution 2.30&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=MF4:TETRAFLUOROMAGNESATE(2-)'>MF4</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=TG1:OCTANOIC ACID [3S-[3ALPHA, 3ABETA, 4ALPHA, 6BETA, 6ABETA, 7BETA, 8ALPHA(Z), 9BALPHA]]-6-(ACETYLOXY)-2,3,-3A,4,5,6,6A,7,8,9B-DECAHYDRO-3,3A-DIHYDROXY-3,6,9-TRIMETHYL-8-[(2-METHYL-1-OXO-2-BUTENYL)OXY]-2-OXO-4-(1-OXOBUTOXY)-AZULENO[4,5-B]FURAN-7-YL ESTER'>TG1</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''Crystal structure of the SR CA2+-ATPase with MGF4'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1WPG 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 <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=MF4:'>MF4</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=TG1:'>TG1</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1WPG OCA].
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1WPG 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=1WPG OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15448704 15448704]
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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]
[[Category: Calcium-transporting ATPase]]
[[Category: Calcium-transporting ATPase]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: p-type atpase]]
[[Category: p-type atpase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:59:57 2008''

Revision as of 13:00, 20 March 2008


PDB ID 1wpg

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands: , , , and
Activity: Calcium-transporting ATPase, with EC number 3.6.3.8
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the SR CA2+-ATPase with MGF4


Overview

P-type ion transporting ATPases are ATP-powered ion pumps that establish ion concentration gradients across biological membranes. Transfer of bound cations to the lumenal or extracellular side occurs while the ATPase is phosphorylated. Here we report at 2.3 A resolution the structure of the calcium-ATPase of skeletal muscle sarcoplasmic reticulum, a representative P-type ATPase that is crystallized in the absence of Ca2+ but in the presence of magnesium fluoride, a stable phosphate analogue. This and other crystal structures determined previously provide atomic models for all four principal states in the reaction cycle. These structures show that the three cytoplasmic domains rearrange to move six out of ten transmembrane helices, thereby changing the affinity of the Ca2+-binding sites and the gating of the ion pathway. Release of ADP triggers the opening of the lumenal gate and release of phosphate its closure, effected mainly through movement of the A-domain, the actuator of transmembrane gates.

About this Structure

1WPG is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

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:15448704

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