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Structural insight into the biogenesis of β-barrel membrane proteins

Author

Listed:
  • Nicholas Noinaj

    (National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health)

  • Adam J. Kuszak

    (National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health)

  • James C. Gumbart

    (School of Physics, Georgia Institute of Technology)

  • Petra Lukacik

    (Diamond Light Source Ltd, Oxfordshire OX11 0DE, UK)

  • Hoshing Chang

    (National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health)

  • Nicole C. Easley

    (National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health)

  • Trevor Lithgow

    (Monash University, Victoria 3800, Australia)

  • Susan K. Buchanan

    (National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health)

Abstract

β-barrel membrane proteins are essential for nutrient import, signalling, motility and survival. In Gram-negative bacteria, the β-barrel assembly machinery (BAM) complex is responsible for the biogenesis of β-barrel membrane proteins, with homologous complexes found in mitochondria and chloroplasts. Here we describe the structure of BamA, the central and essential component of the BAM complex, from two species of bacteria: Neisseria gonorrhoeae and Haemophilus ducreyi. BamA consists of a large periplasmic domain attached to a 16-strand transmembrane β-barrel domain. Three structural features shed light on the mechanism by which BamA catalyses β-barrel assembly. First, the interior cavity is accessible in one BamA structure and conformationally closed in the other. Second, an exterior rim of the β-barrel has a distinctly narrowed hydrophobic surface, locally destabilizing the outer membrane. And third, the β-barrel can undergo lateral opening, suggesting a route from the interior cavity in BamA into the outer membrane.

Suggested Citation

  • Nicholas Noinaj & Adam J. Kuszak & James C. Gumbart & Petra Lukacik & Hoshing Chang & Nicole C. Easley & Trevor Lithgow & Susan K. Buchanan, 2013. "Structural insight into the biogenesis of β-barrel membrane proteins," Nature, Nature, vol. 501(7467), pages 385-390, September.
    • Handle: RePEc:nat:nature:v:501:y:2013:i:7467:d:10.1038_nature12521
    DOI: 10.1038/nature12521
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    Cited by:

    1. Xu Wang & Sarah B. Nyenhuis & Harris D. Bernstein, 2024. "The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Sarah E. Hanson & Tyrone Dowdy & Mioara Larion & Matthew Thomas Doyle & Harris D. Bernstein, 2024. "The patatin-like protein PlpD forms structurally dynamic homodimers in the Pseudomonas aeruginosa outer membrane," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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