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Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM

Author

Listed:
  • Matthew G. Iadanza

    (Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds)

  • Anna J. Higgins

    (Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds)

  • Bob Schiffrin

    (Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds)

  • Antonio N. Calabrese

    (Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds)

  • David J. Brockwell

    (Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds)

  • Alison E. Ashcroft

    (Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds)

  • Sheena E. Radford

    (Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds)

  • Neil A. Ranson

    (Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds)

Abstract

The β-barrel assembly machinery (BAM) is a ∼203 kDa complex of five proteins (BamA–E), which is essential for viability in E. coli. BAM promotes the folding and insertion of β-barrel proteins into the outer membrane via a poorly understood mechanism. Several current models suggest that BAM functions through a ‘lateral gating’ motion of the β-barrel of BamA. Here we present a cryo-EM structure of the BamABCDE complex, at 4.9 Å resolution. The structure is in a laterally open conformation showing that gating is independent of BamB binding. We describe conformational changes throughout the complex and interactions between BamA, B, D and E, and the detergent micelle that suggest communication between BAM and the lipid bilayer. Finally, using an enhanced reconstitution protocol and functional assays, we show that for the outer membrane protein OmpT, efficient folding in vitro requires lateral gating in BAM.

Suggested Citation

  • Matthew G. Iadanza & Anna J. Higgins & Bob Schiffrin & Antonio N. Calabrese & David J. Brockwell & Alison E. Ashcroft & Sheena E. Radford & Neil A. Ranson, 2016. "Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM," Nature Communications, Nature, vol. 7(1), pages 1-12, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12865
    DOI: 10.1038/ncomms12865
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    Cited by:

    1. Dawei Sun & Kelly M. Storek & Dimitry Tegunov & Ying Yang & Christopher P. Arthur & Matthew Johnson & John G. Quinn & Weijing Liu & Guanghui Han & Hany S. Girgis & Mary Kate Alexander & Austin K. Murc, 2024. "The discovery and structural basis of two distinct state-dependent inhibitors of BamA," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Katherine L. Fenn & Jim E. Horne & Joel A. Crossley & Nils Böhringer & Romany J. Horne & Till F. Schäberle & Antonio N. Calabrese & Sheena E. Radford & Neil A. Ranson, 2024. "Outer membrane protein assembly mediated by BAM-SurA complexes," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    3. 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.
    4. Bob Schiffrin & Joel A. Crossley & Martin Walko & Jonathan M. Machin & G. Nasir Khan & Iain W. Manfield & Andrew J. Wilson & David J. Brockwell & Tomas Fessl & Antonio N. Calabrese & Sheena E. Radford, 2024. "Dual client binding sites in the ATP-independent chaperone SurA," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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