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Crystal structure of a catalytic intermediate of the maltose transporter

Author

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  • Michael L. Oldham

    (Department of Biological Sciences,)

  • Dheeraj Khare

    (Department of Biological Sciences,)

  • Florante A. Quiocho

    (Baylor College of Medicine, Houston, Texas 77030, USA)

  • Amy L. Davidson

    (Purdue University, West Lafayette, Indiana 47907, USA)

  • Jue Chen

    (Department of Biological Sciences,)

Abstract

The maltose uptake system of Escherichia coli is a well-characterized member of the ATP-binding cassette transporter superfamily. Here we present the 2.8-Å crystal structure of the intact maltose transporter in complex with the maltose-binding protein, maltose and ATP. This structure, stabilized by a mutation that prevents ATP hydrolysis, captures the ATP-binding cassette dimer in a closed, ATP-bound conformation. Maltose is occluded within a solvent-filled cavity at the interface of the two transmembrane subunits, about halfway into the lipid bilayer. The binding protein docks onto the entrance of the cavity in an open conformation and serves as a cap to ensure unidirectional translocation of the sugar molecule. These results provide direct evidence for a concerted mechanism of transport in which solute is transferred from the binding protein to the transmembrane subunits when the cassette dimer closes to hydrolyse ATP.

Suggested Citation

  • Michael L. Oldham & Dheeraj Khare & Florante A. Quiocho & Amy L. Davidson & Jue Chen, 2007. "Crystal structure of a catalytic intermediate of the maltose transporter," Nature, Nature, vol. 450(7169), pages 515-521, November.
    • Handle: RePEc:nat:nature:v:450:y:2007:i:7169:d:10.1038_nature06264
    DOI: 10.1038/nature06264
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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.
    2. Martin F. Peter & Jan A. Ruland & Peer Depping & Niels Schneberger & Emmanuele Severi & Jonas Moecking & Karl Gatterdam & Sarah Tindall & Alexandre Durand & Veronika Heinz & Jan Peter Siebrasse & Paul, 2022. "Structural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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