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Structure and mechanism of the S component of a bacterial ECF transporter

Author

Listed:
  • Peng Zhang

    (Lewis Thomas Laboratory, Princeton University)

  • Jiawei Wang

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

  • Yigong Shi

    (Ministry of Education Protein Science Laboratory, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University)

Abstract

Vitamin B2 transporter revealed The X-ray crystal structure of a riboflavin (vitamin B2) membrane transporter, a member of the important energy-coupling factor (ECF) family, has been determined. The structure of the membrane-embedded substrate-binding domain of the transporter from Staphylococcus aureus reveals a previously unreported fold, with the riboflavin molecule bound to a loop and to the periplasmic portion of several transmembrane segments.

Suggested Citation

  • Peng Zhang & Jiawei Wang & Yigong Shi, 2010. "Structure and mechanism of the S component of a bacterial ECF transporter," Nature, Nature, vol. 468(7324), pages 717-720, December.
    • Handle: RePEc:nat:nature:v:468:y:2010:i:7324:d:10.1038_nature09488
    DOI: 10.1038/nature09488
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    Cited by:

    1. Chancievan Thangaratnarajah & Mark Nijland & Luís Borges-Araújo & Aike Jeucken & Jan Rheinberger & Siewert J. Marrink & Paulo C. T. Souza & Cristina Paulino & Dirk J. Slotboom, 2023. "Expulsion mechanism of the substrate-translocating subunit in ECF transporters," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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