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Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT

Author

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  • Nien-Jen Hu

    (Imperial College London
    Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Didcot
    Research Complex at Harwell Rutherford, Appleton Laboratory, Harwell)

  • So Iwata

    (Imperial College London
    Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Didcot
    Research Complex at Harwell Rutherford, Appleton Laboratory, Harwell
    Japan Science and Technology Agency, ERATO, Human Crystallography Project, Yoshida Konoe, Sakyo-ku)

  • Alexander D. Cameron

    (Imperial College London
    Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Didcot
    Research Complex at Harwell Rutherford, Appleton Laboratory, Harwell
    Japan Science and Technology Agency, ERATO, Human Crystallography Project, Yoshida Konoe, Sakyo-ku)

  • David Drew

    (Imperial College London)

Abstract

Structure of a bile acid transporter Elevated cholesterol levels significantly increase the risk of atherosclerosis and cardiovascular diseases. Cholesterol is eliminated from the body following conversion to bile acids, so the apical sodium-dependent bile acid transporter (ASBT) that reabsorbs bile acid in the intestine is a major drug target for cholesterol-lowering therapy. The X-ray crystal structure of a bacterial homologue of ASBT bound to its bile acid substrate has now been determined. The substrate (taurocholate) is found in a large hydrophobic cavity between the protein's 'core' and 'panel' domains, suggesting a possible transport mechanism for this important biomolecule.

Suggested Citation

  • Nien-Jen Hu & So Iwata & Alexander D. Cameron & David Drew, 2011. "Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT," Nature, Nature, vol. 478(7369), pages 408-411, October.
    • Handle: RePEc:nat:nature:v:478:y:2011:i:7369:d:10.1038_nature10450
    DOI: 10.1038/nature10450
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    Cited by:

    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. Benedikt T. Kuhn & Jonathan Zöller & Iwan Zimmermann & Tim Gemeinhardt & Dogukan H. Özkul & Julian D. Langer & Markus A. Seeger & Eric R. Geertsma, 2024. "Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    3. Kaho Shionoya & Jae-Hyun Park & Toru Ekimoto & Junko S. Takeuchi & Junki Mifune & Takeshi Morita & Naito Ishimoto & Haruka Umezawa & Kenichiro Yamamoto & Chisa Kobayashi & Atsuto Kusunoki & Norimichi , 2024. "Structural basis for hepatitis B virus restriction by a viral receptor homologue," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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