IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v443y2006i7108d10.1038_nature05155.html
   My bibliography  Save this article

Structure of a bacterial multidrug ABC transporter

Author

Listed:
  • Roger J. P. Dawson

    (Institute of Molecular Biology and Biophysics, ETH Zurich)

  • Kaspar P. Locher

    (Institute of Molecular Biology and Biophysics, ETH Zurich)

Abstract

Multidrug transporters of the ABC family facilitate the export of diverse cytotoxic drugs across cell membranes. This is clinically relevant, as tumour cells may become resistant to agents used in chemotherapy. To understand the molecular basis of this process, we have determined the 3.0 Å crystal structure of a bacterial ABC transporter (Sav1866) from Staphylococcus aureus. The homodimeric protein consists of 12 transmembrane helices in an arrangement that is consistent with cross-linking studies and electron microscopic imaging of the human multidrug resistance protein MDR1, but critically different from that reported for the bacterial lipid flippase MsbA. The observed, outward-facing conformation reflects the ATP-bound state, with the two nucleotide-binding domains in close contact and the two transmembrane domains forming a central cavity—presumably the drug translocation pathway—that is shielded from the inner leaflet of the lipid bilayer and from the cytoplasm, but exposed to the outer leaflet and the extracellular space.

Suggested Citation

  • Roger J. P. Dawson & Kaspar P. Locher, 2006. "Structure of a bacterial multidrug ABC transporter," Nature, Nature, vol. 443(7108), pages 180-185, September.
    • Handle: RePEc:nat:nature:v:443:y:2006:i:7108:d:10.1038_nature05155
    DOI: 10.1038/nature05155
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature05155
    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/nature05155?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. Tianqi Zhang & Jixing Lyu & Bowei Yang & Sangho D. Yun & Elena Scott & Minglei Zhao & Arthur Laganowsky, 2024. "Native mass spectrometry and structural studies reveal modulation of MsbA–nucleotide interactions by lipids," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    2. Lin Yu & Xin Xu & Wan-Zhen Chua & Hao Feng & Zheng Ser & Kai Shao & Jian Shi & Yumei Wang & Zongli Li & Radoslaw M. Sobota & Lok-To Sham & Min Luo, 2023. "Structural basis of peptide secretion for Quorum sensing by ComA," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    3. Adrian W R Serohijos & Tamás Hegedűs & John R Riordan & Nikolay V Dokholyan, 2008. "Diminished Self-Chaperoning Activity of the ΔF508 Mutant of CFTR Results in Protein Misfolding," PLOS Computational Biology, Public Library of Science, vol. 4(2), pages 1-8, February.
    4. Sheng Cao & Yihu Yang & Lili He & Yumo Hang & Xiaodong Yan & Hui Shi & Jiaquan Wu & Zhuqing Ouyang, 2023. "Cryo-EM structures of mitochondrial ABC transporter ABCB10 in apo and biliverdin-bound form," Nature Communications, Nature, vol. 14(1), pages 1-9, December.
    5. Jere P. Segrest & Chongren Tang & Hyun D. Song & Martin K. Jones & W. Sean Davidson & Stephen G. Aller & Jay W. Heinecke, 2022. "ABCA1 is an extracellular phospholipid translocase," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    6. Megan L O’Mara & Alan E Mark, 2014. "Structural Characterization of Two Metastable ATP-Bound States of P-Glycoprotein," PLOS ONE, Public Library of Science, vol. 9(3), pages 1-14, March.

    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:443:y:2006:i:7108:d:10.1038_nature05155. 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.