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Mechanisms of molecular transport through the urea channel of Helicobacter pylori

Author

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  • Reginald McNulty

    (University of California
    Present address: Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California 92037, USA)

  • Jakob P. Ulmschneider

    (Jiao-Tong University)

  • Hartmut Luecke

    (University of California
    3205 McGaugh Hall, University of California
    University of California
    University of California)

  • Martin B. Ulmschneider

    (Johns Hopkins University)

Abstract

Helicobacter pylori survival in acidic environments relies on cytoplasmic hydrolysis of gastric urea into ammonia and carbon dioxide, which buffer the pathogen’s periplasm. Urea uptake is greatly enhanced and regulated by HpUreI, a proton-gated inner membrane channel protein essential for gastric survival of H. pylori. The crystal structure of HpUreI describes a static snapshot of the channel with two constriction sites near the center of the bilayer that are too narrow to allow passage of urea or even water. Here we describe the urea transport mechanism at atomic resolution, revealed by unrestrained microsecond equilibrium molecular dynamics simulations of the hexameric channel assembly. Two consecutive constrictions open to allow conduction of urea, which is guided through the channel by interplay between conserved residues that determine proton rejection and solute selectivity. Remarkably, HpUreI conducts water at rates equivalent to aquaporins, which might be essential for efficient transport of urea at small concentration gradients.

Suggested Citation

  • Reginald McNulty & Jakob P. Ulmschneider & Hartmut Luecke & Martin B. Ulmschneider, 2013. "Mechanisms of molecular transport through the urea channel of Helicobacter pylori," Nature Communications, Nature, vol. 4(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3900
    DOI: 10.1038/ncomms3900
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