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Structural basis for the facilitative diffusion mechanism by SemiSWEET transporter

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  • Yongchan Lee

    (Graduate School of Science, University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan)

  • Tomohiro Nishizawa

    (Graduate School of Science, University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
    Precursory Research for Embryonic Science and Technology (PRESTO), Japan Science and Technology Agency)

  • Keitaro Yamashita

    (RIKEN SPring-8 Center)

  • Ryuichiro Ishitani

    (Graduate School of Science, University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan)

  • Osamu Nureki

    (Graduate School of Science, University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan)

Abstract

SWEET family proteins mediate sugar transport across biological membranes and play crucial roles in plants and animals. The SWEETs and their bacterial homologues, the SemiSWEETs, are related to the PQ-loop family, which is characterized by highly conserved proline and glutamine residues (PQ-loop motif). Although the structures of the bacterial SemiSWEETs were recently reported, the conformational transition and the significance of the conserved motif in the transport cycle have remained elusive. Here we report crystal structures of SemiSWEET from Escherichia coli, in the both inward-open and outward-open states. A structural comparison revealed that SemiSWEET undergoes an intramolecular conformational change in each protomer. The conserved PQ-loop motif serves as a molecular hinge that enables the ‘binder clip-like’ motion of SemiSWEET. The present work provides the framework for understanding the overall transport cycles of SWEET and PQ-loop family proteins.

Suggested Citation

  • Yongchan Lee & Tomohiro Nishizawa & Keitaro Yamashita & Ryuichiro Ishitani & Osamu Nureki, 2015. "Structural basis for the facilitative diffusion mechanism by SemiSWEET transporter," Nature Communications, Nature, vol. 6(1), pages 1-8, May.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7112
    DOI: 10.1038/ncomms7112
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    Cited by:

    1. Jonas C. Alvim & Robert M. Bolt & Jing An & Yasuko Kamisugi & Andrew Cuming & Fernanda A. L. Silva-Alvim & Juan O. Concha & Luis L. P. daSilva & Meiyi Hu & Dominique Hirsz & Jurgen Denecke, 2023. "The K/HDEL receptor does not recycle but instead acts as a Golgi-gatekeeper," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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