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Structure of a fucose transporter in an outward-open conformation

Author

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  • Shangyu Dang

    (State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University)

  • Linfeng Sun

    (State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University)

  • Yongjian Huang

    (State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University)

  • Feiran Lu

    (State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University)

  • Yufeng Liu

    (State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University)

  • Haipeng Gong

    (State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University)

  • Jiawei Wang

    (State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University)

  • Nieng Yan

    (State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University)

Abstract

FucP: an open and shut case MFS (major facilitator superfamily) transporters are an ancient and ubiquitous class of transport protein. After several decades of research, the structures of three MFS transporters were known — LacY and GlpT in an inward-open conformation and EmrD in an intermediate conformation. The lack of a known structure for an MFS transporter in the outward-open conformation has limited the mechanistic understanding of their function. That gap has now been filled with the publication of the structure of FucP, the Escherichia coli transporter responsible for the uptake of L-fucose, an important source of carbon for microorganisms, in the outward-open conformation.

Suggested Citation

  • Shangyu Dang & Linfeng Sun & Yongjian Huang & Feiran Lu & Yufeng Liu & Haipeng Gong & Jiawei Wang & Nieng Yan, 2010. "Structure of a fucose transporter in an outward-open conformation," Nature, Nature, vol. 467(7316), pages 734-738, October.
    • Handle: RePEc:nat:nature:v:467:y:2010:i:7316:d:10.1038_nature09406
    DOI: 10.1038/nature09406
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    Cited by:

    1. Yeonjung Lim & Ji-Hui Seo & Stephen J. Giovannoni & Ilnam Kang & Jang-Cheon Cho, 2023. "Cultivation of marine bacteria of the SAR202 clade," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Basavraj Khanppnavar & Julian Maier & Freja Herborg & Ralph Gradisch & Erika Lazzarin & Dino Luethi & Jae-Won Yang & Chao Qi & Marion Holy & Kathrin Jäntsch & Oliver Kudlacek & Klaus Schicker & Thomas, 2022. "Structural basis of organic cation transporter-3 inhibition," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    3. Jody L. Andersen & Gui-Xin He & Prathusha Kakarla & Ranjana KC & Sanath Kumar & Wazir Singh Lakra & Mun Mun Mukherjee & Indrika Ranaweera & Ugina Shrestha & Thuy Tran & Manuel F. Varela, 2015. "Multidrug Efflux Pumps from Enterobacteriaceae, Vibrio cholerae and Staphylococcus aureus Bacterial Food Pathogens," IJERPH, MDPI, vol. 12(2), pages 1-61, January.

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