2dqs
Crystal structure of the calcium pump with amppcp in the absence of calcium
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OverviewOverview
Calcium ATPase is a member of the P-type ATPases that transport ions, across the membrane against a concentration gradient. Here we have solved, the crystal structure of the calcium ATPase of skeletal muscle, sarcoplasmic reticulum (SERCA1a) at 2.6 A resolution with two calcium ions, bound in the transmembrane domain, which comprises ten alpha-helices. The, two calcium ions are located side by side and are surrounded by four, transmembrane helices, two of which are unwound for efficient coordination, geometry. The cytoplasmic region consists of three well separated domains, with the phosphorylation site in the central catalytic domain and the, adenosine-binding site on another domain. The phosphorylation domain has, the same fold as haloacid dehalogenase. Comparison with a low-resolution, electron density map of the enzyme in the absence of calcium and with, biochemical data suggests that large domain movements take place during, active transport.
About this StructureAbout this Structure
2DQS is a Single protein structure of sequence from Oryctolagus cuniculus with MG, NA, ACP, TG1 and PTY as ligands. Active as Calcium-transporting ATPase, with EC number 3.6.3.8 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution., Toyoshima C, Nakasako M, Nomura H, Ogawa H, Nature. 2000 Jun 8;405(6787):647-55. PMID:10864315
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