Phospholipid flipping involves a central cavity in P4 ATPases.

ABSTRACT: P4 ATPase flippases translocate phospholipids across biomembranes, thus contributing to the establishment of transmembrane lipid asymmetry, a feature important for multiple cellular processes. The mechanism by which such phospholipid flipping occurs remains elusive as P4 ATPases transport a giant substrate very different from that of other P-type ATPases such as Na⁺/K⁺- and Ca²⁺-ATPases. Based on available crystal structures of cation-transporting P-type ATPases, we generated a structural model of the broad-specificity flippase ALA10. In this model, a cavity delimited by transmembrane segments TM3, TM4, and TM5 is present in the transmembrane domain at a similar position as the cation-binding region in related P-type ATPases. Docking of a phosphatidylcholin

SUBMITTER: Jensen MS 

PROVIDER: S-EPMC5732287 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature