6ZHG

Ca2+-ATPase from Listeria Monocytogenes in complex with AlF

Summary for 6ZHG

• Entry DOI: 10.2210/pdb6zhg/pdb
• Descriptor: Calcium-transporting ATPase, TETRAFLUOROALUMINATE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: transport protein p-type atpase ca2+ pump, transport protein
• Biological source: Listeria monocytogenes
• Total number of polymer chains: 1
• Total formula weight: 97554.69

Authors

Basse Hansen, S.,Dyla, M.,Neumann, C.,Quistgaard, E.M.H.,Lauwring Andersen, J.,Kjaergaard, M.,Nissen, P. (deposition date: 2020-06-23, release date: 2021-05-19, Last modification date: 2024-01-24)

Primary citation

Hansen, S.B.,Dyla, M.,Neumann, C.,Quistgaard, E.M.H.,Andersen, J.L.,Kjaergaard, M.,Nissen, P.
The Crystal Structure of the Ca 2+ -ATPase 1 from Listeria monocytogenes reveals a Pump Primed for Dephosphorylation.
J.Mol.Biol., 433:167015-167015, 2021

PubMed Abstract: Many bacteria export intracellular calcium using active transporters homologous to the sarco/endoplasmic reticulum Ca-ATPase (SERCA). Here we present three crystal structures of Ca-ATPase 1 from Listeria monocytogenes (LMCA1). Structures with BeF 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 Ca 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 Ca 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 Ca exchange pathways. The LMCA1 structures provide insight into the evolutionary divergence and conserved features of this important class of ion transporters.

PubMed: 33933469
DOI: 10.1016/j.jmb.2021.167015

Experimental method

X-RAY DIFFRACTION (4 Å)