Structure of the [Ca]E2P intermediate of Ca2+-ATPase 1 from Listeria monocytogenes

ABSTRACT: Active transport by P-type Ca2+-ATPases maintain internal calcium stores and a low cytosolic calcium concentration. Structural studies of mammalian sarco/endoplasmic reticulum Ca2+-ATPases (SERCA) have revealed several steps of the transport cycle, but a calcium releasing intermediate has remained elusive. Single-molecule FRET studies of the bacterial Ca2+-ATPase LMCA1 revealed an intermediate of the transition between so-called [Ca]E1P and E2P states and suggested that calcium release from this intermediate was the essentially irreversible step of transport. Here, we present a 3.5 Å resolution cryo-EM structure for a four-glycine insertion mutant of LMCA1 in a lipid nanodisc obtained under conditions with calcium and ATP and adopting such an intermediate state, denoted [Ca]E2P. The cytoso

SUBMITTER: Poul Nissen 

PROVIDER: S-SCDT-10_1038-S44319-025-00392-X | biostudies-other |

REPOSITORIES: biostudies-other