1vfp
From Proteopedia
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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 CA, MG and ACP 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 Wed Nov 21 04:48:26 2007
