CryoEM structures of P-type ATPases in lipid nanodiscs
Abstract
P-type ATPases are a large family of membrane transporters that use the energy of ATP hydrolysis to transport ions and lipids across biological membranes. Despite extensive research, the regulation of these transporters remains a major question in the field. While it is known that lipid composition affects P-type ATPase function, the precise impact on their structural and dynamic behavior is not fully understood. In this study, we reconstituted Ca2+-ATPase (LMCA1) into lipid bilayer nanodiscs and observed that LMCA1 exhibits maximum activity in anionic POPG lipid membranes. We will use single-particle cryo-electron microscopy (cryo-EM) to determine the structures of LMCA1 in different intermediate states in lipid nanodiscs. A successful Cryo-EM experiment on LMCA1 nanodiscs will provide valuable insights into the structural dynamics and mechanism of action of P-type ATPases in their native membrane environment.
