Structure and Mechanism of P-Type ATPase Ion Pumps

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Structure and Mechanism of P-Type ATPase Ion Pumps. / Dyla, Mateusz; Kjærgaard, Magnus; Poulsen, Hanne; Nissen, Poul.

In: Annual Review of Biochemistry, Vol. 89, 06.2020, p. 583-603.

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@article{3008f7c7f25e47ddba3192184892ee10,
title = "Structure and Mechanism of P-Type ATPase Ion Pumps",
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. Expected final online publication date for the Annual Review of Biochemistry, Volume 89 is June 22, 2020. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.",
author = "Mateusz Dyla and Magnus Kj{\ae}rgaard and Hanne Poulsen and Poul Nissen",
year = "2020",
month = jun,
doi = "10.1146/annurev-biochem-010611-112801",
language = "English",
volume = "89",
pages = "583--603",
journal = "Annual Review of Biochemistry",
issn = "0066-4154",
publisher = "Annual Reviews",

}

RIS

TY - JOUR

T1 - Structure and Mechanism of P-Type ATPase Ion Pumps

AU - Dyla, Mateusz

AU - Kjærgaard, Magnus

AU - Poulsen, Hanne

AU - Nissen, Poul

PY - 2020/6

Y1 - 2020/6

N2 - 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. Expected final online publication date for the Annual Review of Biochemistry, Volume 89 is June 22, 2020. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

AB - 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. Expected final online publication date for the Annual Review of Biochemistry, Volume 89 is June 22, 2020. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

U2 - 10.1146/annurev-biochem-010611-112801

DO - 10.1146/annurev-biochem-010611-112801

M3 - Journal article

C2 - 31874046

VL - 89

SP - 583

EP - 603

JO - Annual Review of Biochemistry

JF - Annual Review of Biochemistry

SN - 0066-4154

ER -