Copper-transporting P-type ATPases use a unique ion-release pathway

Biochemical characterization of P-type copper ATPases

Copper ATPases, in analogy with other members of the P-ATPase superfamily, contain a catalytic headpiece including an aspartate residue reacting with ATP to form a phosphoenzyme intermediate, and transmembrane helices containing cation-binding sites [TMBS (transmembrane metal-binding sites)] for catalytic activation and cation translocation. Following phosphoenzyme formation by utilization of A...

Ion Motive ATPases: V- and P-type ATPases

Biological membranes are composed of phospholipid bilayers and mark the boundaries between the cell or organelle and its exterior. There is little, if any, free diffusion of ions or hydrophilic solutes across phospholipid bilayers. Thus, to enable the cell to control the composition of its intracellular environment, nature has evolved membrane proteins that form specialized pathways across them...

Families of soft-metal-ion-transporting ATPases.

Function and regulation of human copper-transporting ATPases.

Copper-transporting ATPases (Cu-ATPases) ATP7A and ATP7B are evolutionarily conserved polytopic membrane proteins with essential roles in human physiology. The Cu-ATPases are expressed in most tissues, and their transport activity is crucial for central nervous system development, liver function, connective tissue formation, and many other physiological processes. The loss of ATP7A or ATP7B fun...

Evolution of Copper Transporting ATPases in Eukaryotic Organisms

Copper is an essential nutrient for most life forms, however in excess it can be harmful. The ATP-driven copper pumps (Copper-ATPases) play critical role in living organisms by maintaining appropriate copper levels in cells and tissues. These evolutionary conserved polytopic membrane proteins are present in all phyla from simplest life forms (bacteria) to highly evolved eukaryotes (Homo sapiens...