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Crystal structure of a bacterial homologue of glucose transporters GLUT1–4

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  • Linfeng Sun

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

  • Xin Zeng

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

  • Chuangye Yan

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

  • Xiuyun Sun

    (School of Life Sciences and School of Medicine, Tsinghua University)

  • Xinqi Gong

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

  • Yu Rao

    (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, Tsinghua University
    School of Life Sciences and School of Medicine, Tsinghua University
    Tsinghua-Peking Center for Life Sciences, Tsinghua University)

Abstract

Glucose transporters are essential for metabolism of glucose in cells of diverse organisms from microbes to humans, exemplified by the disease-related human proteins GLUT1, 2, 3 and 4. Despite rigorous efforts, the structural information for GLUT1–4 or their homologues remains largely unknown. Here we report three related crystal structures of XylE, an Escherichia coli homologue of GLUT1–4, in complex with d-xylose, d-glucose and 6-bromo-6-deoxy-d-glucose, at resolutions of 2.8, 2.9 and 2.6 Å, respectively. The structure consists of a typical major facilitator superfamily fold of 12 transmembrane segments and a unique intracellular four-helix domain. XylE was captured in an outward-facing, partly occluded conformation. Most of the important amino acids responsible for recognition of d-xylose or d-glucose are invariant in GLUT1–4, suggesting functional and mechanistic conservations. Structure-based modelling of GLUT1–4 allows mapping and interpretation of disease-related mutations. The structural and biochemical information reported here constitutes an important framework for mechanistic understanding of glucose transporters and sugar porters in general.

Suggested Citation

  • Linfeng Sun & Xin Zeng & Chuangye Yan & Xiuyun Sun & Xinqi Gong & Yu Rao & Nieng Yan, 2012. "Crystal structure of a bacterial homologue of glucose transporters GLUT1–4," Nature, Nature, vol. 490(7420), pages 361-366, October.
  • Handle: RePEc:nat:nature:v:490:y:2012:i:7420:d:10.1038_nature11524
    DOI: 10.1038/nature11524
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    Cited by:

    1. Nan Wang & Shuo Zhang & Yafei Yuan & Hanwen Xu & Elisabeth Defossa & Hans Matter & Melissa Besenius & Volker Derdau & Matthias Dreyer & Nis Halland & Kaihui Hu He & Stefan Petry & Michael Podeschwa & , 2022. "Molecular basis for inhibiting human glucose transporters by exofacial inhibitors," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    2. Monique R Heitmeier & Richard C Hresko & Rachel L Edwards & Michael J Prinsen & Ma Xenia G Ilagan & Audrey R Odom John & Paul W Hruz, 2019. "Identification of druggable small molecule antagonists of the Plasmodium falciparum hexose transporter PfHT and assessment of ligand access to the glucose permeation pathway via FLAG-mediated protein ," PLOS ONE, Public Library of Science, vol. 14(5), pages 1-20, May.
    3. Chen Ling & George L. Peabody & Davinia Salvachúa & Young-Mo Kim & Colin M. Kneucker & Christopher H. Calvey & Michela A. Monninger & Nathalie Munoz Munoz & Brenton C. Poirier & Kelsey J. Ramirez & Pe, 2022. "Muconic acid production from glucose and xylose in Pseudomonas putida via evolution and metabolic engineering," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    4. Albert Suades & Aziz Qureshi & Sarah E. McComas & Mathieu Coinçon & Axel Rudling & Yurie Chatzikyriakidou & Michael Landreh & Jens Carlsson & David Drew, 2023. "Establishing mammalian GLUT kinetics and lipid composition influences in a reconstituted-liposome system," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    5. Elisabeth Lambert & Ahmad Reza Mehdipour & Alexander Schmidt & Gerhard Hummer & Camilo Perez, 2022. "Evidence for a trap-and-flip mechanism in a proton-dependent lipid transporter," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    6. 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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