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The structural basis of proton driven zinc transport by ZntB

Author

Listed:
  • Cornelius Gati

    (Francis Crick Avenue, Cambridge Biomedical Campus)

  • Artem Stetsenko

    (Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen)

  • Dirk J. Slotboom

    (Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen)

  • Sjors H. W. Scheres

    (Francis Crick Avenue, Cambridge Biomedical Campus)

  • Albert Guskov

    (Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen)

Abstract

Zinc is an essential microelement to sustain all forms of life. However, excess of zinc is toxic, therefore dedicated import, export and storage proteins for tight regulation of the zinc concentration have evolved. In Enterobacteriaceae, several membrane transporters are involved in zinc homeostasis and linked to virulence. ZntB has been proposed to play a role in the export of zinc, but the transport mechanism of ZntB is poorly understood and based only on experimental characterization of its distant homologue CorA magnesium channel. Here, we report the cryo-electron microscopy structure of full-length ZntB from Escherichia coli together with the results of isothermal titration calorimetry, and radio-ligand uptake and fluorescent transport assays on ZntB reconstituted into liposomes. Our results show that ZntB mediates Zn2+ uptake, stimulated by a pH gradient across the membrane, using a transport mechanism that does not resemble the one proposed for homologous CorA channels.

Suggested Citation

  • Cornelius Gati & Artem Stetsenko & Dirk J. Slotboom & Sjors H. W. Scheres & Albert Guskov, 2017. "The structural basis of proton driven zinc transport by ZntB," Nature Communications, Nature, vol. 8(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01483-7
    DOI: 10.1038/s41467-017-01483-7
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    Cited by:

    1. Louis Tung Faat Lai & Jayashree Balaraman & Fei Zhou & Doreen Matthies, 2023. "Cryo-EM structures of human magnesium channel MRS2 reveal gating and regulatory mechanisms," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    2. Ming Li & Yang Li & Yue Lu & Jianhui Li & Xuhang Lu & Yue Ren & Tianlei Wen & Yaojie Wang & Shenghai Chang & Xing Zhang & Xue Yang & Yuequan Shen, 2023. "Molecular basis of Mg2+ permeation through the human mitochondrial Mrs2 channel," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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