The Crystal Structure of the Ca2+-ATPase 1 from Listeria monocytogenes reveals a Pump Primed for Dephosphorylation
| Autor: | C. Neumann, Poul Nissen, Sara Basse Hansen, Mateusz Dyla, Magnus Kjaergaard, Esben M. Quistgaard, Jacob Andersen |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
SERCA
Listeria ATPase chemistry.chemical_element Calcium Calcium in biology Ca-ATPase LMCA1 membrane protein crystallography Dephosphorylation 03 medical and health sciences 0302 clinical medicine Ion binding Structural Biology P-type ATPase ddc:610 Binding site Molecular Biology Ion transporter 030304 developmental biology 0303 health sciences calcium biology Chemistry Endoplasmic reticulum Biophysics biology.protein 030217 neurology & neurosurgery |
| Zdroj: | Hansen, S B, Dyla, M, Neumann, C, Quistgaard, E M H, Andersen, J L, Kjaergaard, M & Nissen, P 2021, ' The Crystal Structure of the Ca 2+-ATPase 1 from Listeria monocytogenes reveals a Pump Primed for Dephosphorylation ', Journal of Molecular Biology, vol. 433, no. 16, 167015 . https://doi.org/10.1016/j.jmb.2021.167015 Journal of molecular biology 433(16), 167015 (2021). doi:10.1016/j.jmb.2021.167015 |
| DOI: | 10.1016/j.jmb.2021.167015 |
| Popis: | Journal of molecular biology 433(16), 167015 (2021). doi:10.1016/j.jmb.2021.167015 Many bacteria export intracellular calcium using active transporters homologous to the sarco/endoplasmic reticulum Ca$^{2+}$-ATPase (SERCA). Here we present three crystal structures of Ca$^{2+}$-ATPase 1 from Listeria monocytogenes (LMCA1). Structures with BeF$^{-}_{3}$- 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$^{2+}$ 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$^{2+}$ 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$^{2+}$ exchange pathways. The LMCA1 structures provide insight into the evolutionary divergence and conserved features of this important class of ion transporters. Published by Elsevier, Amsterdam [u.a.] |
| Databáze: | OpenAIRE |
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