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Mechanism of substrate recognition and transport by an amino acid antiporter

Author

Listed:
  • Xiang Gao

    (Ministry of Education Protein Science Laboratory,)

  • Lijun Zhou

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China)

  • Xuyao Jiao

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China
    School of Life Sciences, Shandong University, Jinan, Shandong 250100, China)

  • Feiran Lu

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China)

  • Chuangye Yan

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China)

  • Xin Zeng

    (Ministry of Education Protein Science Laboratory,)

  • Jiawei Wang

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China)

  • Yigong Shi

    (Ministry of Education Protein Science Laboratory,)

Abstract

Amino acid antiporter recognition mechanisms Some bacteria rely on the amino acid antiporter AdiC to expel protons by exchanging intracellular agmatine for extracellular arginine. The structure of the substrate-free form of AdiC is known, and it is believed to represent an 'outward-open' conformation. In this study, Gao et al. solved the X-ray crystal structure of an AdiC variant bound to Arg. The positively charged Arg is enclosed in an acidic binding chamber, with the head groups of Arg hydrogen bonded to main chain atoms of AdiC and the aliphatic portion of Arg stacked by hydrophobic side chains of highly conserved residues. The authors identified three potential gates, involving four aromatic residues and Glu 208, which may work in concert to differentially regulate the upload and release of Arg and Agm.

Suggested Citation

  • Xiang Gao & Lijun Zhou & Xuyao Jiao & Feiran Lu & Chuangye Yan & Xin Zeng & Jiawei Wang & Yigong Shi, 2010. "Mechanism of substrate recognition and transport by an amino acid antiporter," Nature, Nature, vol. 463(7282), pages 828-832, February.
  • Handle: RePEc:nat:nature:v:463:y:2010:i:7282:d:10.1038_nature08741
    DOI: 10.1038/nature08741
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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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