The Crystal Structure of the Ca2+-ATPase 1 from Listeria monocytogenes reveals a Pump Primed for Dephosphorylation

Sara Basse Hansen, Mateusz Dyla, Caroline Neumann, Esben Meldgaard Hoegh Quistgaard, Jacob Lauwring Andersen, Magnus Kjaergaard, Poul Nissen*

*Corresponding author for this work

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Many bacteria export intracellular calcium using active transporters homologous to the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA). Here we present three crystal structures of Ca2+-ATPase 1 from Listeria monocytogenes (LMCA1). Structures with BeF3- mimicking a phosphoenzyme state reveal a closed state, which is intermediate between the outward-open E2P and the proton-occluded E2-P* conformations known for SERCA. It suggests that LMCA1 in the E2P state is pre-organized for dephosphorylation upon Ca2+ release, consistent with the rapid dephosphorylation observed in single-molecule studies. An arginine side-chain occupies the position equivalent to calcium binding site I in SERCA, leaving a single Ca2+ binding site in LMCA1, corresponding to SERCA site II. Observing no putative transport pathways dedicated to protons, we infer a direct proton counter transport through the Ca2+ exchange pathways. The LMCA1 structures provide insight into the evolutionary divergence and conserved features of this important class of ion transporters.

Original languageEnglish
Article number167015
JournalJournal of Molecular Biology
Publication statusPublished - Aug 2021


  • Ca-ATPase LMCA1
  • calcium
  • Listeria
  • membrane protein crystallography
  • P-type ATPase

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