Structure and Mechanism of P-Type ATPase Ion Pumps

Mateusz Dyla; Magnus Kjærgaard; Hanne Poulsen; Poul Nissen

doi:10.1146/annurev-biochem-010611-112801

Structure and Mechanism of P-Type ATPase Ion Pumps

Annu Rev Biochem. 2020 Jun 20:89:583-603. doi: 10.1146/annurev-biochem-010611-112801. Epub 2020 Dec 24.

Authors

Mateusz Dyla^{1

2}, Magnus Kjærgaard^{1

2}, Hanne Poulsen^{1

2}, Poul Nissen^{1

2}

Affiliations

¹ Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus, Denmark; email: [email protected].
² Danish Research Institute of Translational Neuroscience (DANDRITE), Nordic European Molecular Biology Laboratory (EMBL) Partnership for Molecular Medicine, 8000 Aarhus, Denmark.

PMID: 31874046
DOI: 10.1146/annurev-biochem-010611-112801

Abstract

P-type ATPases are found in all kingdoms of life and constitute a wide range of cation transporters, primarily for H⁺, Na⁺, K⁺, Ca²⁺, and transition metal ions such as Cu(I), Zn(II), and Cd(II). They have been studied through a wide range of techniques, and research has gained very significant insight on their transport mechanism and regulation. Here, we review the structure, function, and dynamics of P2-ATPases including Ca²⁺-ATPases and Na,K-ATPase. We highlight mechanisms of functional transitions that are associated with ion exchange on either side of the membrane and how the functional cycle is regulated by interaction partners, autoregulatory domains, and off-cycle states. Finally, we discuss future perspectives based on emerging techniques and insights.

Keywords: Ca2+-ATPase; Na,K-ATPase; autoinhibition; intrinsically disordered; membrane transport protein; single molecule.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Adenosine Triphosphate / chemistry*
Adenosine Triphosphate / metabolism
Animals
Binding Sites
Cations, Divalent
Cations, Monovalent
Copper-Transporting ATPases / chemistry*
Copper-Transporting ATPases / genetics
Copper-Transporting ATPases / metabolism
H(+)-K(+)-Exchanging ATPase / chemistry*
H(+)-K(+)-Exchanging ATPase / genetics
H(+)-K(+)-Exchanging ATPase / metabolism
Humans
Ion Transport
Models, Molecular
Protein Binding
Protein Interaction Domains and Motifs
Protein Structure, Secondary
Protons
Sarcoplasmic Reticulum Calcium-Transporting ATPases / chemistry*
Sarcoplasmic Reticulum Calcium-Transporting ATPases / genetics
Sarcoplasmic Reticulum Calcium-Transporting ATPases / metabolism
Single Molecule Imaging
Sodium-Potassium-Exchanging ATPase / chemistry*
Sodium-Potassium-Exchanging ATPase / genetics
Sodium-Potassium-Exchanging ATPase / metabolism
Substrate Specificity

Substances

Cations, Divalent
Cations, Monovalent
Protons
Adenosine Triphosphate
H(+)-K(+)-Exchanging ATPase
Sarcoplasmic Reticulum Calcium-Transporting ATPases
Sodium-Potassium-Exchanging ATPase
Copper-Transporting ATPases