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Structure of a prokaryotic virtual proton pump at 3.2 Å resolution

Author

Listed:
  • Yiling Fang

    (Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA)

  • Hariharan Jayaram

    (Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA)

  • Tania Shane

    (Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA)

  • Ludmila Kolmakova-Partensky

    (Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA)

  • Fang Wu

    (Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA)

  • Carole Williams

    (Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA)

  • Yong Xiong

    (Yale University, New Haven, Connecticut 06520, USA)

  • Christopher Miller

    (Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA)

Abstract

The AdiC proton pump Little is known about the structure of the APC superfamily of membrane proteins, which transport amino acids, polyamines and cations in a variety of physiological contexts. Here, Fang et al. report the 3.2 Å crystal structure of AdiC, an arginine–agmatine antiporter from Escherichia coli. The protein, which is captured in a substrate-free outward-facing conformation, has the same structural fold as a number of Na+-coupled transporter families. Fang et al. also demonstrate that each subunit of AdiC functions independently.

Suggested Citation

  • Yiling Fang & Hariharan Jayaram & Tania Shane & Ludmila Kolmakova-Partensky & Fang Wu & Carole Williams & Yong Xiong & Christopher Miller, 2009. "Structure of a prokaryotic virtual proton pump at 3.2 Å resolution," Nature, Nature, vol. 460(7258), pages 1040-1043, August.
    • Handle: RePEc:nat:nature:v:460:y:2009:i:7258:d:10.1038_nature08201
    DOI: 10.1038/nature08201
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    Cited by:

    1. Yaning Li & Yingying Guo & Angelika Bröer & Lu Dai & Stefan Brӧer & Renhong Yan, 2024. "Cryo-EM structure of the human Asc-1 transporter complex," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
    2. Joanne L. Parker & Justin C. Deme & Dimitrios Kolokouris & Gabriel Kuteyi & Philip C. Biggin & Susan M. Lea & Simon Newstead, 2021. "Molecular basis for redox control by the human cystine/glutamate antiporter system xc−," Nature Communications, Nature, vol. 12(1), pages 1-11, December.

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