1vfp
From Proteopedia
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- | [[Image:1vfp.jpg|left|200px]] | + | [[Image:1vfp.jpg|left|200px]] |
- | + | ||
- | '''Crystal structure of the SR CA2+-ATPase with bound AMPPCP''' | + | {{Structure |
+ | |PDB= 1vfp |SIZE=350|CAPTION= <scene name='initialview01'>1vfp</scene>, resolution 2.90Å | ||
+ | |SITE= | ||
+ | |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> | ||
+ | |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] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of the SR CA2+-ATPase with bound AMPPCP''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1VFP is a [ | + | 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== | ||
- | 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:// | + | 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]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''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
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, resolution 2.90Å | |||||||
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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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