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Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE

Author

Listed:
  • Goragot Wisedchaisri

    (Janelia Research Campus, Howard Hughes Medical Institute)

  • Min-Sun Park

    (Janelia Research Campus, Howard Hughes Medical Institute)

  • Matthew G. Iadanza

    (Janelia Research Campus, Howard Hughes Medical Institute)

  • Hongjin Zheng

    (Janelia Research Campus, Howard Hughes Medical Institute)

  • Tamir Gonen

    (Janelia Research Campus, Howard Hughes Medical Institute)

Abstract

The major facilitator superfamily (MFS) is the largest collection of structurally related membrane proteins that transport a wide array of substrates. The proton-coupled sugar transporter XylE is the first member of the MFS that has been structurally characterized in multiple transporting conformations, including both the outward and inward-facing states. Here we report the crystal structure of XylE in a new inward-facing open conformation, allowing us to visualize the rocker-switch movement of the N-domain against the C-domain during the transport cycle. Using molecular dynamics simulation, and functional transport assays, we describe the movement of XylE that facilitates sugar translocation across a lipid membrane and identify the likely candidate proton-coupling residues as the conserved Asp27 and Arg133. This study addresses the structural basis for proton-coupled substrate transport and release mechanism for the sugar porter family of proteins.

Suggested Citation

  • Goragot Wisedchaisri & Min-Sun Park & Matthew G. Iadanza & Hongjin Zheng & Tamir Gonen, 2014. "Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE," Nature Communications, Nature, vol. 5(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5521
    DOI: 10.1038/ncomms5521
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    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. Reza Dastvan & Ali Rasouli & Sepehr Dehghani-Ghahnaviyeh & Samantha Gies & Emad Tajkhorshid, 2022. "Proton-driven alternating access in a spinster lipid transporter," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    3. 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.
    4. Sille Remm & Dario Vecchis & Jendrik Schöppe & Cedric A. J. Hutter & Imre Gonda & Michael Hohl & Simon Newstead & Lars V. Schäfer & Markus A. Seeger, 2023. "Structural basis for triacylglyceride extraction from mycobacterial inner membrane by MFS transporter Rv1410," Nature Communications, Nature, vol. 14(1), pages 1-17, December.

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