6ZHH
Ca2+-ATPase from Listeria Monocytogenes with G4 insertion.
Summary for 6ZHH
| Entry DOI | 10.2210/pdb6zhh/pdb |
| Descriptor | Calcium-transporting ATPase, BERYLLIUM TRIFLUORIDE ION, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | p-type atpase calcium pump, listeria monocytogenes, transport protein |
| Biological source | Listeria monocytogenes |
| Total number of polymer chains | 8 |
| Total formula weight | 810992.10 |
| 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 Cited by 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: 33933469DOI: 10.1016/j.jmb.2021.167015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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