1vfp
From Proteopedia
(New page: 200px<br /><applet load="1vfp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vfp, resolution 2.90Å" /> '''Crystal structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1vfp.jpg|left|200px]]<br /><applet load="1vfp" size=" | + | [[Image:1vfp.jpg|left|200px]]<br /><applet load="1vfp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vfp, resolution 2.90Å" /> | caption="1vfp, resolution 2.90Å" /> | ||
'''Crystal structure of the SR CA2+-ATPase with bound AMPPCP'''<br /> | '''Crystal structure of the SR CA2+-ATPase with bound AMPPCP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | P-type ATPases are ATP-powered ion pumps that establish ion concentration | + | 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== | ==About this Structure== | ||
| - | 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 CA, MG and ACP 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:// | + | 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]. |
==Reference== | ==Reference== | ||
| Line 23: | Line 23: | ||
[[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 15:34:50 2008'' |
Revision as of 13:34, 21 February 2008
|
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 with , and as ligands. Active as Calcium-transporting ATPase, with EC number 3.6.3.8 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
Page seeded by OCA on Thu Feb 21 15:34:50 2008
