Chemicals and Drugs [D] » Enzymes and Coenzymes [D08] » Enzymes » Hydrolases » Acid Anhydride Hydrolases » Adenosine Triphosphatases » P-type ATPases
Chemicals and Drugs [D] » Amino Acids, Peptides, and Proteins [D12] » Proteins » Carrier Proteins » Membrane Transport Proteins » P-type ATPases
Chemicals and Drugs [D] » Amino Acids, Peptides, and Proteins [D12] » Proteins » Membrane Proteins » Membrane Transport Proteins » P-type ATPases
Description
A highly conserved family of ATPases that facilitate the transport of lipids and cations across the plasma membrane. Structurally, they are elongated ALPHA-HELICES constituting five functionally distinct domains: three cytoplasmic domains A, N, and P which contain the catalytic sites, and two transmembrane domains. The N domain phosphorylates the P-domain at an invariant ASPARTATE residue, which, in turn, is dephosphorylated by the A domain. The phosphorylation and dephosphorylation cycles drive conformational changes in the protein between two states (E1 and E2), which allow the substrate to access the other side of the membrane. MeSH
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