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Molecular insights into substrate translocation in an elevator-type metal transporter

Author

Listed:
  • Yao Zhang

    (Michigan State University)

  • Majid Jafari

    (Michigan State University)

  • Tuo Zhang

    (Michigan State University
    China Agricultural University)

  • Dexin Sui

    (Michigan State University)

  • Luca Sagresti

    (Scuola Normale Superiore
    Istituto Nazionale di Fisica Nucleare (INFN) sezione di Pisa)

  • Kenneth M. Merz

    (Michigan State University
    Michigan State University
    The Cleveland Clinic)

  • Jian Hu

    (Michigan State University
    Michigan State University)

Abstract

The Zrt/Irt-like protein (ZIP) metal transporters are key players in maintaining the homeostasis of a panel of essential microelements. The prototypical ZIP from Bordetella bronchiseptica (BbZIP) is an elevator transporter, but how the metal substrate moves along the transport pathway and how the transporter changes conformation to allow alternating access remain to be elucidated. Here, we combine structural, biochemical, and computational approaches to investigate the process of metal substrate translocation along with the global structural rearrangement. Our study reveals an upward hinge motion of the transport domain in a high-resolution crystal structure of a cross-linked variant, elucidates the mechanisms of metal release from the transport site into the cytoplasm and activity regulation by a cytoplasmic metal-binding loop, and unravels an unusual elevator mode in enhanced sampling simulations that distinguishes BbZIP from other elevator transporters. This work provides important insights into the metal transport mechanism of the ZIP family.

Suggested Citation

  • Yao Zhang & Majid Jafari & Tuo Zhang & Dexin Sui & Luca Sagresti & Kenneth M. Merz & Jian Hu, 2024. "Molecular insights into substrate translocation in an elevator-type metal transporter," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
  • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-54048-w
    DOI: 10.1038/s41467-024-54048-w
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    References listed on IDEAS

    as
    1. Yao Zhang & Yuhan Jiang & Kaifu Gao & Dexin Sui & Peixuan Yu & Min Su & Guo-Wei Wei & Jian Hu, 2023. "Structural insights into the elevator-type transport mechanism of a bacterial ZIP metal transporter," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    2. Tuo Zhang & Dexin Sui & Jian Hu, 2016. "Structural insights of ZIP4 extracellular domain critical for optimal zinc transport," Nature Communications, Nature, vol. 7(1), pages 1-13, September.
    3. Javier Abellon-Ruiz & Kalyanashis Jana & Augustinas Silale & Andrew M. Frey & Arnaud Baslé & Matthias Trost & Ulrich Kleinekathöfer & Bert Berg, 2023. "BtuB TonB-dependent transporters and BtuG surface lipoproteins form stable complexes for vitamin B12 uptake in gut Bacteroides," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    4. Changxu Pang & Jin Chai & Ping Zhu & John Shanklin & Qun Liu, 2023. "Structural mechanism of intracellular autoregulation of zinc uptake in ZIP transporters," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    5. Lan Zhao & Eduardo Oliver & Klio Maratou & Santosh S. Atanur & Olivier D. Dubois & Emanuele Cotroneo & Chien-Nien Chen & Lei Wang & Cristina Arce & Pauline L. Chabosseau & Joan Ponsa-Cobas & Maria G. , 2015. "The zinc transporter ZIP12 regulates the pulmonary vascular response to chronic hypoxia," Nature, Nature, vol. 524(7565), pages 356-360, August.
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