IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v463y2010i7282d10.1038_nature08741.html
   My bibliography  Save this article

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
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature08741
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature08741?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    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.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:463:y:2010:i:7282:d:10.1038_nature08741. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.