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Crystal structure of a phosphorylation-coupled saccharide transporter

Author

Listed:
  • Yu Cao

    (College of Physicians and Surgeons, Columbia University)

  • Xiangshu Jin

    (Center for Computational Biology and Bioinformatics, Howard Hughes Medical Institute, Columbia University)

  • Elena J. Levin

    (College of Physicians and Surgeons, Columbia University)

  • Hua Huang

    (College of Physicians and Surgeons, Columbia University)

  • Yinong Zong

    (Sanford-Burnham Institute)

  • Matthias Quick

    (Columbia University
    New York State Psychiatric Institute, 1051 Riverside Drive)

  • Jun Weng

    (College of Physicians and Surgeons, Columbia University)

  • Yaping Pan

    (College of Physicians and Surgeons, Columbia University)

  • James Love

    (New York Consortium on Membrane Protein Structure, New York Structural Biology Center)

  • Marco Punta

    (New York Consortium on Membrane Protein Structure, New York Structural Biology Center
    Technical University of Munich)

  • Burkhard Rost

    (New York Consortium on Membrane Protein Structure, New York Structural Biology Center
    Technical University of Munich)

  • Wayne A. Hendrickson

    (New York Consortium on Membrane Protein Structure, New York Structural Biology Center
    Howard Hughes Medical Institute, Columbia University)

  • Jonathan A. Javitch

    (Columbia University
    New York State Psychiatric Institute, 1051 Riverside Drive
    Columbia University)

  • Kanagalaghatta R. Rajashankar

    (Cornell University, NE-CAT, Advanced Photon Source)

  • Ming Zhou

    (College of Physicians and Surgeons, Columbia University)

Abstract

Saccharides have a central role in the nutrition of all living organisms. Whereas several saccharide uptake systems are shared between the different phylogenetic kingdoms, the phosphoenolpyruvate-dependent phosphotransferase system exists almost exclusively in bacteria. This multi-component system includes an integral membrane protein EIIC that transports saccharides and assists in their phosphorylation. Here we present the crystal structure of an EIIC from Bacillus cereus that transports diacetylchitobiose. The EIIC is a homodimer, with an expansive interface formed between the amino-terminal halves of the two protomers. The carboxy-terminal half of each protomer has a large binding pocket that contains a diacetylchitobiose, which is occluded from both sides of the membrane with its site of phosphorylation near the conserved His 250 and Glu 334 residues. The structure shows the architecture of this important class of transporters, identifies the determinants of substrate binding and phosphorylation, and provides a framework for understanding the mechanism of sugar translocation.

Suggested Citation

  • Yu Cao & Xiangshu Jin & Elena J. Levin & Hua Huang & Yinong Zong & Matthias Quick & Jun Weng & Yaping Pan & James Love & Marco Punta & Burkhard Rost & Wayne A. Hendrickson & Jonathan A. Javitch & Kana, 2011. "Crystal structure of a phosphorylation-coupled saccharide transporter," Nature, Nature, vol. 473(7345), pages 50-54, May.
    • Handle: RePEc:nat:nature:v:473:y:2011:i:7345:d:10.1038_nature09939
    DOI: 10.1038/nature09939
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    Cited by:

    1. Iven Winkelmann & Povilas Uzdavinys & Ian M. Kenney & Joseph Brock & Pascal F. Meier & Lina-Marie Wagner & Florian Gabriel & Sukkyeong Jung & Rei Matsuoka & Christoph Ballmoos & Oliver Beckstein & Dav, 2022. "Crystal structure of the Na+/H+ antiporter NhaA at active pH reveals the mechanistic basis for pH sensing," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Patrick Roth & Jean-Marc Jeckelmann & Inken Fender & Zöhre Ucurum & Thomas Lemmin & Dimitrios Fotiadis, 2024. "Structure and mechanism of a phosphotransferase system glucose transporter," Nature Communications, Nature, vol. 15(1), pages 1-10, December.

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