Structural dynamics of P-type ATPase ion pumps

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisReviewForskningpeer review

Standard

Structural dynamics of P-type ATPase ion pumps. / Dyla, Mateusz; Basse Hansen, Sara; Nissen, Poul; Kjaergaard, Magnus.

I: Biochemical Society Transactions, Bind 47, Nr. 5, 31.10.2019, s. 1247-1257.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisReviewForskningpeer review

Harvard

APA

CBE

MLA

Dyla, Mateusz o.a.. "Structural dynamics of P-type ATPase ion pumps". Biochemical Society Transactions. 2019, 47(5). 1247-1257. https://doi.org/10.1042/BST20190124

Vancouver

Author

Dyla, Mateusz ; Basse Hansen, Sara ; Nissen, Poul ; Kjaergaard, Magnus. / Structural dynamics of P-type ATPase ion pumps. I: Biochemical Society Transactions. 2019 ; Bind 47, Nr. 5. s. 1247-1257.

Bibtex

@article{7ab22cd627444fa1a8bf94afbaad47d6,
title = "Structural dynamics of P-type ATPase ion pumps",
abstract = "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 F{\"o}rster 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.",
keywords = "dynamics, LMCA1, P-type ATPase, SERCA, smFRET",
author = "Mateusz Dyla and {Basse Hansen}, Sara and Poul Nissen and Magnus Kjaergaard",
year = "2019",
month = oct,
day = "31",
doi = "10.1042/BST20190124",
language = "English",
volume = "47",
pages = "1247--1257",
journal = "Biochemical Society. Transactions",
issn = "0300-5127",
publisher = "Portland Press Ltd.",
number = "5",

}

RIS

TY - JOUR

T1 - Structural dynamics of P-type ATPase ion pumps

AU - Dyla, Mateusz

AU - Basse Hansen, Sara

AU - Nissen, Poul

AU - Kjaergaard, Magnus

PY - 2019/10/31

Y1 - 2019/10/31

N2 - 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.

AB - 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.

KW - dynamics

KW - LMCA1

KW - P-type ATPase

KW - SERCA

KW - smFRET

UR - http://www.scopus.com/inward/record.url?scp=85074414717&partnerID=8YFLogxK

U2 - 10.1042/BST20190124

DO - 10.1042/BST20190124

M3 - Review

C2 - 31671180

AN - SCOPUS:85074414717

VL - 47

SP - 1247

EP - 1257

JO - Biochemical Society. Transactions

JF - Biochemical Society. Transactions

SN - 0300-5127

IS - 5

ER -