Structural identification of cation binding pockets in the plasma membrane proton pump

Kira Ekberg; Bjørn Panella Pedersen; Danny Mollerup Sørensen; Ann Kallehauge Nielsen; Bjarke Veierskov; Poul Nissen; Michael Broberg Palmgren; Morten Jeppe Buch-Pedersen

doi:10.1073/pnas.1010416107

Structural identification of cation binding pockets in the plasma membrane proton pump

Kira Ekberg, Bjørn Panella Pedersen, Danny Mollerup Sørensen, Ann Kallehauge Nielsen, Bjarke Veierskov, Poul Nissen, Michael Broberg Palmgren, Morten Jeppe Buch-Pedersen

11 Citations (Scopus)

Abstract

The activity of P-type plasma membrane H⁺-ATPases is modulated by H⁺ and cations, with K⁺ and Ca²⁺ being of physiological relevance. Using X-ray crystallography, we have located the binding site for Rb⁺ as a K⁺ congener, and for Tb ³⁺ and Ho³⁺ as Ca²⁺ congeners. Rb⁺ is found coordinated by a conserved aspartate residue in the phosphorylation domain. A single Tb³⁺ ion is identified positioned in the nucleotide-binding domain in close vicinity to the bound nucleotide. Ho ³⁺ ions are coordinated at two distinct sites within the H ⁺-ATPase: One site is at the interface of the nucleotidebinding and phosphorylation domains, and the other is in the transmembrane domain toward the extracellular side. The identified binding sites are suggested to represent binding pockets for regulatory cations and a H⁺ binding site for protons leaving the pump molecule. This implicates Ho³⁺ as a novel chemical tool for identification of proton binding sites.

Original language	English
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	107
Issue number	50
Pages (from-to)	21400-21405
Number of pages	6
ISSN	0027-8424
DOIs	https://doi.org/10.1073/pnas.1010416107
Publication status	Published - 14 Dec 2010

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Structural identification of cation binding pockets in the plasma membrane proton pump. / Ekberg, Kira; Pedersen, Bjørn Panella; Sørensen, Danny Mollerup et al.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 107, No. 50, 14.12.2010, p. 21400-21405.

Research output: Contribution to journal › Journal article › Research › peer-review

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title = "Structural identification of cation binding pockets in the plasma membrane proton pump",

abstract = "The activity of P-type plasma membrane H+-ATPases is modulated by H+ and cations, with K+ and Ca2+ being of physiological relevance. Using X-ray crystallography, we have located the binding site for Rb+ as a K+ congener, and for Tb 3+ and Ho3+ as Ca2+ congeners. Rb+ is found coordinated by a conserved aspartate residue in the phosphorylation domain. A single Tb3+ ion is identified positioned in the nucleotide-binding domain in close vicinity to the bound nucleotide. Ho 3+ ions are coordinated at two distinct sites within the H +-ATPase: One site is at the interface of the nucleotidebinding and phosphorylation domains, and the other is in the transmembrane domain toward the extracellular side. The identified binding sites are suggested to represent binding pockets for regulatory cations and a H+ binding site for protons leaving the pump molecule. This implicates Ho3+ as a novel chemical tool for identification of proton binding sites.",

author = "Kira Ekberg and Pedersen, {Bj{\o}rn Panella} and S{\o}rensen, {Danny Mollerup} and Nielsen, {Ann Kallehauge} and Bjarke Veierskov and Poul Nissen and Palmgren, {Michael Broberg} and Buch-Pedersen, {Morten Jeppe}",

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T1 - Structural identification of cation binding pockets in the plasma membrane proton pump

AU - Ekberg, Kira

AU - Pedersen, Bjørn Panella

AU - Sørensen, Danny Mollerup

AU - Nielsen, Ann Kallehauge

AU - Veierskov, Bjarke

AU - Nissen, Poul

AU - Palmgren, Michael Broberg

AU - Buch-Pedersen, Morten Jeppe

PY - 2010/12/14

Y1 - 2010/12/14

N2 - The activity of P-type plasma membrane H+-ATPases is modulated by H+ and cations, with K+ and Ca2+ being of physiological relevance. Using X-ray crystallography, we have located the binding site for Rb+ as a K+ congener, and for Tb 3+ and Ho3+ as Ca2+ congeners. Rb+ is found coordinated by a conserved aspartate residue in the phosphorylation domain. A single Tb3+ ion is identified positioned in the nucleotide-binding domain in close vicinity to the bound nucleotide. Ho 3+ ions are coordinated at two distinct sites within the H +-ATPase: One site is at the interface of the nucleotidebinding and phosphorylation domains, and the other is in the transmembrane domain toward the extracellular side. The identified binding sites are suggested to represent binding pockets for regulatory cations and a H+ binding site for protons leaving the pump molecule. This implicates Ho3+ as a novel chemical tool for identification of proton binding sites.

AB - The activity of P-type plasma membrane H+-ATPases is modulated by H+ and cations, with K+ and Ca2+ being of physiological relevance. Using X-ray crystallography, we have located the binding site for Rb+ as a K+ congener, and for Tb 3+ and Ho3+ as Ca2+ congeners. Rb+ is found coordinated by a conserved aspartate residue in the phosphorylation domain. A single Tb3+ ion is identified positioned in the nucleotide-binding domain in close vicinity to the bound nucleotide. Ho 3+ ions are coordinated at two distinct sites within the H +-ATPase: One site is at the interface of the nucleotidebinding and phosphorylation domains, and the other is in the transmembrane domain toward the extracellular side. The identified binding sites are suggested to represent binding pockets for regulatory cations and a H+ binding site for protons leaving the pump molecule. This implicates Ho3+ as a novel chemical tool for identification of proton binding sites.

U2 - 10.1073/pnas.1010416107

DO - 10.1073/pnas.1010416107

M3 - Journal article

C2 - 21098259

SN - 0027-8424

VL - 107

SP - 21400

EP - 21405

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 50

ER -

Structural identification of cation binding pockets in the plasma membrane proton pump

Abstract

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