1iwo

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(New page: 200px<br /> <applet load="1iwo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iwo, resolution 3.10&Aring;" /> '''Crystal structure o...)
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[[Image:1iwo.gif|left|200px]]<br /><applet load="1iwo" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1iwo" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1iwo, resolution 3.10&Aring;" />
caption="1iwo, resolution 3.10&Aring;" />
'''Crystal structure of the SR Ca2+-ATPase in the absence of Ca2+'''<br />
'''Crystal structure of the SR Ca2+-ATPase in the absence of Ca2+'''<br />
==Overview==
==Overview==
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In skeletal muscle, calcium ions are transported (pumped) against a, concentration gradient from the cytoplasm into the sarcoplasmic reticulum, an intracellular organelle. This causes muscle cells to relax after, cytosolic calcium increases during excitation. The Ca(2+) ATPase that, carries out this pumping is a representative P-type ion-transporting, ATPase. Here we describe the structure of this ion pump at 3.1 A, resolution in a Ca(2+)-free (E2) state, and compare it with that, determined previously for the Ca(2+)-bound (E1Ca(2+)) state. The structure, of the enzyme stabilized by thapsigargin, a potent inhibitor, shows large, conformation differences from that in E1Ca(2+). Three cytoplasmic domains, gather to form a single headpiece, and six of the ten transmembrane, helices exhibit large-scale rearrangements. These rearrangements ensure, the release of calcium ions into the lumen of sarcoplasmic reticulum and, on the cytoplasmic side, create a pathway for entry of new calcium ions.
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In skeletal muscle, calcium ions are transported (pumped) against a concentration gradient from the cytoplasm into the sarcoplasmic reticulum, an intracellular organelle. This causes muscle cells to relax after cytosolic calcium increases during excitation. The Ca(2+) ATPase that carries out this pumping is a representative P-type ion-transporting ATPase. Here we describe the structure of this ion pump at 3.1 A resolution in a Ca(2+)-free (E2) state, and compare it with that determined previously for the Ca(2+)-bound (E1Ca(2+)) state. The structure of the enzyme stabilized by thapsigargin, a potent inhibitor, shows large conformation differences from that in E1Ca(2+). Three cytoplasmic domains gather to form a single headpiece, and six of the ten transmembrane helices exhibit large-scale rearrangements. These rearrangements ensure the release of calcium ions into the lumen of sarcoplasmic reticulum and, on the cytoplasmic side, create a pathway for entry of new calcium ions.
==About this Structure==
==About this Structure==
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1IWO 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 TG1 as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1IWO with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb51_1.html The Calcium Pump]]. 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=1IWO OCA].
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1IWO 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=TG1:'>TG1</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1IWO with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb51_1.html The Calcium Pump]]. 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=1IWO OCA].
==Reference==
==Reference==
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[[Category: p-type atpase]]
[[Category: p-type atpase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:02:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:16:26 2008''

Revision as of 11:16, 21 February 2008


1iwo, resolution 3.10Å

Drag the structure with the mouse to rotate

Crystal structure of the SR Ca2+-ATPase in the absence of Ca2+

Overview

In skeletal muscle, calcium ions are transported (pumped) against a concentration gradient from the cytoplasm into the sarcoplasmic reticulum, an intracellular organelle. This causes muscle cells to relax after cytosolic calcium increases during excitation. The Ca(2+) ATPase that carries out this pumping is a representative P-type ion-transporting ATPase. Here we describe the structure of this ion pump at 3.1 A resolution in a Ca(2+)-free (E2) state, and compare it with that determined previously for the Ca(2+)-bound (E1Ca(2+)) state. The structure of the enzyme stabilized by thapsigargin, a potent inhibitor, shows large conformation differences from that in E1Ca(2+). Three cytoplasmic domains gather to form a single headpiece, and six of the ten transmembrane helices exhibit large-scale rearrangements. These rearrangements ensure the release of calcium ions into the lumen of sarcoplasmic reticulum and, on the cytoplasmic side, create a pathway for entry of new calcium ions.

About this Structure

1IWO is a Single protein structure of sequence from Oryctolagus cuniculus with as ligand. The following page contains interesting information on the relation of 1IWO with [The Calcium Pump]. Active as Calcium-transporting ATPase, with EC number 3.6.3.8 Full crystallographic information is available from OCA.

Reference

Structural changes in the calcium pump accompanying the dissociation of calcium., Toyoshima C, Nomura H, Nature. 2002 Aug 8;418(6898):605-11. PMID:12167852

Page seeded by OCA on Thu Feb 21 13:16:26 2008

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