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The structure of the KtrAB potassium transporter

Author

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  • Ricardo S. Vieira-Pires

    (IBMC, Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre 823, Porto 4150-180, Portugal)

  • Andras Szollosi

    (IBMC, Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre 823, Porto 4150-180, Portugal)

  • João H. Morais-Cabral

    (IBMC, Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre 823, Porto 4150-180, Portugal)

Abstract

In bacteria, archaea, fungi and plants the Trk, Ktr and HKT ion transporters are key components of osmotic regulation, pH homeostasis and resistance to drought and high salinity. These ion transporters are functionally diverse: they can function as Na+ or K+ channels and possibly as cation/K+ symporters. They are closely related to potassium channels both at the level of the membrane protein and at the level of the cytosolic regulatory domains. Here we describe the crystal structure of a Ktr K+ transporter, the KtrAB complex from Bacillus subtilis. The structure shows the dimeric membrane protein KtrB assembled with a cytosolic octameric KtrA ring bound to ATP, an activating ligand. A comparison between the structure of KtrAB–ATP and the structures of the isolated full-length KtrA protein with ATP or ADP reveals a ligand-dependent conformational change in the octameric ring, raising new ideas about the mechanism of activation in these transporters.

Suggested Citation

  • Ricardo S. Vieira-Pires & Andras Szollosi & João H. Morais-Cabral, 2013. "The structure of the KtrAB potassium transporter," Nature, Nature, vol. 496(7445), pages 323-328, April.
    • Handle: RePEc:nat:nature:v:496:y:2013:i:7445:d:10.1038_nature12055
    DOI: 10.1038/nature12055
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    Cited by:

    1. Wesley Tien Chiang & Yao-Kai Chang & Wei-Han Hui & Shu-Wei Chang & Chen-Yi Liao & Yi-Chuan Chang & Chun-Jung Chen & Wei-Chen Wang & Chien-Chen Lai & Chun-Hsiung Wang & Siou-Ying Luo & Ya-Ping Huang & , 2024. "Structural basis and synergism of ATP and Na+ activation in bacterial K+ uptake system KtrAB," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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