1vfp

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[[Image:1vfp.jpg|left|200px]]<br /><applet load="1vfp" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1vfp.jpg|left|200px]]
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caption="1vfp, resolution 2.90&Aring;" />
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'''Crystal structure of the SR CA2+-ATPase with bound AMPPCP'''<br />
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{{Structure
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|PDB= 1vfp |SIZE=350|CAPTION= <scene name='initialview01'>1vfp</scene>, resolution 2.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER'>ACP</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 bound AMPPCP'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ACP:'>ACP</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=1VFP OCA].
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1VFP 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=1VFP OCA].
==Reference==
==Reference==
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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]
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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://www.ncbi.nlm.nih.gov/pubmed/15229613 15229613]
[[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 15:34:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:44:56 2008''

Revision as of 12:45, 20 March 2008


PDB ID 1vfp

Drag the structure with the mouse to rotate
, resolution 2.90Å
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 bound AMPPCP


Overview

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

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

Reference

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

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