1wpg
From Proteopedia
(New page: 200px<br /><applet load="1wpg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wpg, resolution 2.30Å" /> '''Crystal structure of...) |
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| - | [[Image:1wpg.jpg|left|200px]]<br /><applet load="1wpg" size=" | + | [[Image:1wpg.jpg|left|200px]]<br /><applet load="1wpg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wpg, resolution 2.30Å" /> | caption="1wpg, resolution 2.30Å" /> | ||
'''Crystal structure of the SR CA2+-ATPase with MGF4'''<br /> | '''Crystal structure of the SR CA2+-ATPase with MGF4'''<br /> | ||
==Overview== | ==Overview== | ||
| - | P-type ion transporting ATPases are ATP-powered ion pumps that establish | + | 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== | ==About this Structure== | ||
| - | 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 MG, NA, MF4, ADP and TG1 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: p-type atpase]] | [[Category: p-type atpase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:51 2008'' |
Revision as of 13:46, 21 February 2008
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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 with , , , and as ligands. Active as Calcium-transporting ATPase, with EC number 3.6.3.8 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
Page seeded by OCA on Thu Feb 21 15:46:51 2008
Categories: Calcium-transporting ATPase | Oryctolagus cuniculus | Single protein | Nomura, H. | Toyoshima, C. | Tsuda, T. | ADP | MF4 | MG | NA | TG1 | Had fold | Membrane protein | P-type atpase
