6ZHF

Calcium ATPase-1 from Listeria monocytogenes in complex with BeF

6ZHF の概要

• エントリーDOI: 10.2210/pdb6zhf/pdb
• 分子名称: Calcium-transporting ATPase, MAGNESIUM ION, BERYLLIUM TRIFLUORIDE ION, ... (4 entities in total)
• 機能のキーワード: p-type atpase calcium pump listeria monocytogenes, transport protein
• 由来する生物種: Listeria monocytogenes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 97517.72

構造登録者

Basse Hansen, S.,Dyla, M.,Neumann, C.,Quistgaard, E.M.H.,Lauwring Andersen, J.,Kjaergaard, M.,Nissen, P. (登録日: 2020-06-23, 公開日: 2021-05-19, 最終更新日: 2024-01-24)

主引用文献

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

実験手法

X-RAY DIFFRACTION (4 Å)