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

Publikováno v: 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

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

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https://pure.au.dk/portal/da/publications/the-crystal-structure-of-the-ca2atpase-1-from-listeria-monocytogenes-reveals-a-pump-primed-for-dephosphorylation(0f720282-27dd-4d8f-8b0c-3ac08bac9f0b).html

Structural dynamics of P-type ATPase ion pumps

Autor: Magnus Kjaergaard, Poul Nissen, Mateusz Dyla, Sara Basse Hansen

Publikováno v: Dyla, M, Basse Hansen, S, Nissen, P & Kjaergaard, M 2019, ' Structural dynamics of P-type ATPase ion pumps ', Biochemical Society Transactions, vol. 47, no. 5, pp. 1247-1257 . https://doi.org/10.1042/BST20190124

P-type ATPases transport ions across biological membranes against concentration gradients and are essential for all cells. They use the energy from ATP hydrolysis to propel large intramolecular movements, which drive vectorial transport of ions. Tigh

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::941982bc6506a088b26403f77396f0c9
https://pubmed.ncbi.nlm.nih.gov/31671180