Poul Nissen

Crystal structure of the sodium-potassium pump

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Crystal structure of the sodium-potassium pump. / Morth, J Preben; Pedersen, Bjørn Panyella; Toustrup-Jensen, Mads S; Sørensen, Thomas L-M; Petersen, Janne; Andersen, Jens Peter; Vilsen, Bente; Nissen, Poul.

In: Nature, Vol. 450, No. 7172, 2007, p. 1043-1049.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

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Morth, J Preben et al. "Crystal structure of the sodium-potassium pump". Nature. 2007, 450(7172). 1043-1049. https://doi.org/10.1038/nature06419

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@article{6a3132e0dd9f11dc9e31000ea68e967b,
title = "Crystal structure of the sodium-potassium pump",
abstract = "The Na+,K+-ATPase generates electrochemical gradients for sodium and potassium that are vital to animal cells, exchanging three sodium ions for two potassium ions across the plasma membrane during each cycle of ATP hydrolysis. Here we present the X-ray crystal structure at 3.5 A resolution of the pig renal Na+,K+-ATPase with two rubidium ions bound (as potassium congeners) in an occluded state in the transmembrane part of the alpha-subunit. Several of the residues forming the cavity for rubidium/potassium occlusion in the Na+,K+-ATPase are homologous to those binding calcium in the Ca2+-ATPase of sarco(endo)plasmic reticulum. The beta- and gamma-subunits specific to the Na+,K+-ATPase are associated with transmembrane helices alphaM7/alphaM10 and alphaM9, respectively. The gamma-subunit corresponds to a fragment of the V-type ATPase c subunit. The carboxy terminus of the alpha-subunit is contained within a pocket between transmembrane helices and seems to be a novel regulatory element controlling sodium affinity, possibly influenced by the membrane potential.",
keywords = "Adenosine Triphosphate, Animals, Binding Sites, Cations, Monovalent, Cell Membrane, Crystallization, Crystallography, X-Ray, Fluorides, Kidney, Magnesium Compounds, Membrane Potentials, Models, Molecular, Potassium, Protein Subunits, Sodium, Sodium-Potassium-Exchanging ATPase, Swine",
author = "Morth, {J Preben} and Pedersen, {Bj{\o}rn Panyella} and Toustrup-Jensen, {Mads S} and S{\o}rensen, {Thomas L-M} and Janne Petersen and Andersen, {Jens Peter} and Bente Vilsen and Poul Nissen",
year = "2007",
doi = "10.1038/nature06419",
language = "English",
volume = "450",
pages = "1043--1049",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "7172",

}

RIS

TY - JOUR

T1 - Crystal structure of the sodium-potassium pump

AU - Morth, J Preben

AU - Pedersen, Bjørn Panyella

AU - Toustrup-Jensen, Mads S

AU - Sørensen, Thomas L-M

AU - Petersen, Janne

AU - Andersen, Jens Peter

AU - Vilsen, Bente

AU - Nissen, Poul

PY - 2007

Y1 - 2007

N2 - The Na+,K+-ATPase generates electrochemical gradients for sodium and potassium that are vital to animal cells, exchanging three sodium ions for two potassium ions across the plasma membrane during each cycle of ATP hydrolysis. Here we present the X-ray crystal structure at 3.5 A resolution of the pig renal Na+,K+-ATPase with two rubidium ions bound (as potassium congeners) in an occluded state in the transmembrane part of the alpha-subunit. Several of the residues forming the cavity for rubidium/potassium occlusion in the Na+,K+-ATPase are homologous to those binding calcium in the Ca2+-ATPase of sarco(endo)plasmic reticulum. The beta- and gamma-subunits specific to the Na+,K+-ATPase are associated with transmembrane helices alphaM7/alphaM10 and alphaM9, respectively. The gamma-subunit corresponds to a fragment of the V-type ATPase c subunit. The carboxy terminus of the alpha-subunit is contained within a pocket between transmembrane helices and seems to be a novel regulatory element controlling sodium affinity, possibly influenced by the membrane potential.

AB - The Na+,K+-ATPase generates electrochemical gradients for sodium and potassium that are vital to animal cells, exchanging three sodium ions for two potassium ions across the plasma membrane during each cycle of ATP hydrolysis. Here we present the X-ray crystal structure at 3.5 A resolution of the pig renal Na+,K+-ATPase with two rubidium ions bound (as potassium congeners) in an occluded state in the transmembrane part of the alpha-subunit. Several of the residues forming the cavity for rubidium/potassium occlusion in the Na+,K+-ATPase are homologous to those binding calcium in the Ca2+-ATPase of sarco(endo)plasmic reticulum. The beta- and gamma-subunits specific to the Na+,K+-ATPase are associated with transmembrane helices alphaM7/alphaM10 and alphaM9, respectively. The gamma-subunit corresponds to a fragment of the V-type ATPase c subunit. The carboxy terminus of the alpha-subunit is contained within a pocket between transmembrane helices and seems to be a novel regulatory element controlling sodium affinity, possibly influenced by the membrane potential.

KW - Adenosine Triphosphate

KW - Animals

KW - Binding Sites

KW - Cations, Monovalent

KW - Cell Membrane

KW - Crystallization

KW - Crystallography, X-Ray

KW - Fluorides

KW - Kidney

KW - Magnesium Compounds

KW - Membrane Potentials

KW - Models, Molecular

KW - Potassium

KW - Protein Subunits

KW - Sodium

KW - Sodium-Potassium-Exchanging ATPase

KW - Swine

U2 - 10.1038/nature06419

DO - 10.1038/nature06419

M3 - Journal article

C2 - 18075585

VL - 450

SP - 1043

EP - 1049

JO - Nature

JF - Nature

SN - 0028-0836

IS - 7172

ER -