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Plasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM.

Wu R, Bakelar JW, Lundquist K, Zhang Z, Kuo KM, Ryoo D, Pang YT, Sun C, White T, Klose T, Jiang W, Gumbart JC, Noinaj N
Nat Commun 12 7131 (2021)
Related entries: 7ri5, 7ri6, 7ri7, 7ri8, 7ri9, 7rj5

Cited: 15 times
EuropePMC logo PMID: 34880256

Abstract

In Gram-negative bacteria, the biogenesis of β-barrel outer membrane proteins is mediated by the β-barrel assembly machinery (BAM). The mechanism employed by BAM is complex and so far- incompletely understood. Here, we report the structures of BAM in nanodiscs, prepared using polar lipids and native membranes, where we observe an outward-open state. Mutations in the barrel domain of BamA reveal that plasticity in BAM is essential, particularly along the lateral seam of the barrel domain, which is further supported by molecular dynamics simulations that show conformational dynamics in BAM are modulated by the accessory proteins. We also report the structure of BAM in complex with EspP, which reveals an early folding intermediate where EspP threads from the underside of BAM and incorporates into the barrel domain of BamA, supporting a hybrid-barrel budding mechanism in which the substrate is folded into the membrane sequentially rather than as a single unit.

Reviews citing this publication (2)

  1. Surveying membrane landscapes: a new look at the bacterial cell surface. Lithgow T, Stubenrauch CJ, Stumpf MPH. Nat Rev Microbiol (2023)
  2. Targeting BAM for Novel Therapeutics against Pathogenic Gram-Negative Bacteria. Overly Cottom C, Stephenson R, Wilson L, Noinaj N. Antibiotics (Basel) 12 679 (2023)

Articles citing this publication (13)

  1. Uncovering the folding mechanism of pertactin: A comparative study of isolated and vectorial folding. Pang YT, Hazel AJ, Gumbart JC. Biophys J 122 2988-2995 (2023)
  2. Cryo-EM structures reveal multiple stages of bacterial outer membrane protein folding. Doyle MT, Jimah JR, Dowdy T, Ohlemacher SI, Larion M, Hinshaw JE, Bernstein HD. Cell 185 1143-1156.e13 (2022)
  3. Divide and Conquer: A Tailored Solid-state NMR Approach to Study Large Membrane Protein Complexes. Xiang S, Pinto C, Baldus M. Angew Chem Int Ed Engl 61 e202203319 (2022)
  4. FkpA enhances membrane protein folding using an extensive interaction surface. Devlin T, Marx DC, Roskopf MA, Bubb QR, Plummer AM, Fleming KG. Protein Sci 32 e4592 (2023)
  5. A multipoint guidance mechanism for β-barrel folding on the SAM complex. Takeda H, Busto JV, Lindau C, Tsutsumi A, Tomii K, Imai K, Yamamori Y, Hirokawa T, Motono C, Ganesan I, Wenz LS, Becker T, Kikkawa M, Pfanner N, Wiedemann N, Endo T. Nat Struct Mol Biol 30 176-187 (2023)
  6. BamE directly interacts with BamA and BamD coordinating their functions. Kumar S, Konovalova A. Mol Microbiol 120 397-407 (2023)
  7. Cracking outer membrane biogenesis. Guest RL, Silhavy TJ. Biochim Biophys Acta Mol Cell Res 1870 119405 (2023)
  8. Drug Binding to BamA Targets Its Lateral Gate. Kuo KM, Liu J, Pavlova A, Gumbart JC. J Phys Chem B 127 7509-7517 (2023)
  9. Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding. Schiffrin B, Machin JM, Karamanos TK, Zhuravleva A, Brockwell DJ, Radford SE, Calabrese AN. Commun Biol 5 560 (2022)
  10. Factors That Control the Force Needed to Unfold a Membrane Protein in Silico Depend on the Mode of Denaturation. Faruk NF, Peng X, Sosnick TR. Int J Mol Sci 24 2654 (2023)
  11. Large-Scale Conformational Changes of FhaC Provide Insights Into the Two-Partner Secretion Mechanism. Sicoli G, Konijnenberg A, Guérin J, Hessmann S, Del Nero E, Hernandez-Alba O, Lecher S, Rouaut G, Müggenburg L, Vezin H, Cianférani S, Sobott F, Schneider R, Jacob-Dubuisson F. Front Mol Biosci 9 950871 (2022)
  12. Modeling intermediates of BamA folding an outer membrane protein. Kuo KM, Ryoo D, Lundquist K, Gumbart JC. Biophys J 121 3242-3252 (2022)
  13. Structural basis of BAM-mediated outer membrane β-barrel protein assembly. Shen C, Chang S, Luo Q, Chan KC, Zhang Z, Luo B, Xie T, Lu G, Zhu X, Wei X, Dong C, Zhou R, Zhang X, Tang X, Dong H. Nature 617 185-193 (2023)


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