Structural dynamics of P-type ATPase ion pumps
| Autor: | Magnus Kjaergaard, Poul Nissen, Mateusz Dyla, Sara Basse Hansen |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
SERCA
Protein Conformation ATPase LMCA1 Ion Pumps Biochemistry Catalysis Sarcoplasmic Reticulum Calcium-Transporting ATPases Molecular dynamics Ion binding Adenosine Triphosphate ATP hydrolysis P-type ATPase Animals Humans Phosphorylation biology Chemistry Hydrolysis dynamics smFRET Isoenzymes Membrane Förster resonance energy transfer Biophysics biology.protein Calcium Protein Binding |
| Zdroj: | 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 |
| ISSN: | 1470-8752 |
| DOI: | 10.1042/BST20190124 |
| Popis: | 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. Tight coordination of the motions of the pump is required to couple the two spatially distant processes of ion binding and ATP hydrolysis. Here, we review our current understanding of the structural dynamics of P-type ATPases, focusing primarily on Ca2+ pumps. We integrate different types of information that report on structural dynamics, primarily time-resolved fluorescence experiments including single-molecule Förster resonance energy transfer and molecular dynamics simulations, and interpret them in the framework provided by the numerous crystal structures of sarco/endoplasmic reticulum Ca2+-ATPase. We discuss the challenges in characterizing the dynamics of membrane pumps, and the likely impact of new technologies on the field. |
| Databáze: | OpenAIRE |
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