A calcium pump made visible.
The first high-resolution structure of a P-type ATPase, that of the Ca(2+)-ATPase of skeletal muscle sarcoplasmic reticulum, was published in 2000. This structure has provided many clues to how the Ca(2+)-ATPase might work, but no complete answers. The Ca(2+)-ATPase structure reveals no clear pathway from the cytoplasmic side of the membrane to the pair of high-affinity binding sites for Ca(2+) located in the transmembrane region of the ATPase and no clear pathway from these sites to the lumenal side of the membrane. The ATPase is therefore very unlike an ion channel in its construction. It is unclear from the crystal structure of the Ca(2+)-ATPase exactly how the protein sits within the lipid bilayer that surrounds it in the membrane. The Ca(2+)-ATPase is implicated in thermogenesis in some types of muscle; this could involve processes of slippage and leak modulated by interaction between the Ca(2+)-ATPase and sarcolipin.
Lee
Anthony G
AG
Division of Biochemistry and Molecular Biology, School of Biological Sciences, University of Southampton, UK. agl@soton.ac.uk
D001693:Biological Transport, Active; D002118:Calcium / Q000737:chemistry*; D000252:Calcium-Transporting ATPases / Q000737:chemistry* / Q000502:physiology* / Q000648:ultrastructure; D008565:Membrane Proteins / Q000737:chemistry; D008956:Models, Chemical; D008958:Models, Molecular; D010766:Phosphorylation; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D013329:Structure-Activity Relationship
D008565:Membrane Proteins; D000252:Calcium-Transporting ATPases; D002118:Calcium