8bo2 Citations

Structural basis of BAM-mediated outer membrane β-barrel protein assembly.

Nature 617 185-193 (2023)
Related entries: 7ye4, 7ye6, 8bnz

Cited: 16 times
EuropePMC logo PMID: 37100902

Abstract

The outer membrane structure is common in Gram-negative bacteria, mitochondria and chloroplasts, and contains outer membrane β-barrel proteins (OMPs) that are essential interchange portals of materials1-3. All known OMPs share the antiparallel β-strand topology4, implicating a common evolutionary origin and conserved folding mechanism. Models have been proposed for bacterial β-barrel assembly machinery (BAM) to initiate OMP folding5,6; however, mechanisms by which BAM proceeds to complete OMP assembly remain unclear. Here we report intermediate structures of BAM assembling an OMP substrate, EspP, demonstrating sequential conformational dynamics of BAM during the late stages of OMP assembly, which is further supported by molecular dynamics simulations. Mutagenic in vitro and in vivo assembly assays reveal functional residues of BamA and EspP for barrel hybridization, closure and release. Our work provides novel insights into the common mechanism of OMP assembly.

Reviews citing this publication (3)

  1. Biogenesis of mitochondrial β-barrel membrane proteins. Ganesan I, Busto JV, Pfanner N, Wiedemann N. FEBS Open Bio 14 1595-1609 (2024)
  2. ATP-independent assembly machinery of bacterial outer membranes: BAM complex structure and function set the stage for next-generation therapeutics. George A, Patil AG, Mahalakshmi R. Protein Sci 33 e4896 (2024)
  3. Seeing is believing: Illuminating the Gram-negative outer membrane with molecular dynamics simulations. Gutishvili G, Yang L, Gumbart JC. Curr Opin Struct Biol 87 102828 (2024)

Articles citing this publication (13)

  1. Drug Binding to BamA Targets Its Lateral Gate. Kuo KM, Liu J, Pavlova A, Gumbart JC. J Phys Chem B 127 7509-7517 (2023)
  2. BamE directly interacts with BamA and BamD coordinating their functions. Kumar S, Konovalova A. Mol Microbiol 120 397-407 (2023)
  3. Dual recognition of multiple signals in bacterial outer membrane proteins enhances assembly and maintains membrane integrity. Germany EM, Thewasano N, Imai K, Maruno Y, Bamert RS, Stubenrauch CJ, Dunstan RA, Ding Y, Nakajima Y, Lai X, Webb CT, Hidaka K, Tan KS, Shen H, Lithgow T, Shiota T. Elife 12 RP90274 (2024)
  4. Lateral gating mechanism and plasticity of the β-barrel assembly machinery complex in micelles and Escherichia coli. Gopinath A, Rath T, Morgner N, Joseph B. PNAS Nexus 3 pgae019 (2024)
  5. A minimum functional form of the Escherichia coli BAM complex constituted by BamADE assembles outer membrane proteins in vitro. Wang Z, Chu Y, Li Q, Han X, Zhao L, Zhang H, Cai K, Zhang X, Wang X, Qin Y, Fan E. J Biol Chem 300 107324 (2024)
  6. Leptospira interrogans encodes a canonical BamA and three novel noNterm Omp85 outer membrane protein paralogs. Bettin EB, Grassmann AA, Dellagostin OA, Gogarten JP, Caimano MJ. Sci Rep 14 19958 (2024)
  7. Native β-barrel substrates pass through two shared intermediates during folding on the BAM complex. Dos Santos TMA, Thomson BD, Marquez MD, Pan L, Monfared TH, Kahne DE. Proc Natl Acad Sci U S A 121 e2409672121 (2024)
  8. Outer membrane protein assembly mediated by BAM-SurA complexes. Fenn KL, Horne JE, Crossley JA, Böhringer N, Horne RJ, Schäberle TF, Calabrese AN, Radford SE, Ranson NA. Nat Commun 15 7612 (2024)
  9. POTRA domains of the TamA insertase interact with the outer membrane and modulate membrane properties. Mellouk A, Jaouen P, Ruel LJ, Lê M, Martini C, Moraes TF, El Bakkouri M, Lagüe P, Boisselier E, Calmettes C. Proc Natl Acad Sci U S A 121 e2402543121 (2024)
  10. Recent Advances in Modeling Membrane β-Barrel Proteins Using Molecular Dynamics Simulations: From Their Lipid Environments to Their Assemblies. Duncan AL, Gao Y, Haanappel E, Im W, Chavent M. Methods Mol Biol 2778 311-330 (2024)
  11. The discovery and structural basis of two distinct state-dependent inhibitors of BamA. Sun D, Storek KM, Tegunov D, Yang Y, Arthur CP, Johnson M, Quinn JG, Liu W, Han G, Girgis HS, Alexander MK, Murchison AK, Shriver S, Tam C, Ijiri H, Inaba H, Sano T, Yanagida H, Nishikawa J, Heise CE, Fairbrother WJ, Tan MW, Skelton N, Sandoval W, Sellers BD, Ciferri C, Smith PA, Reid PC, Cunningham CN, Rutherford ST, Payandeh J. Nat Commun 15 8718 (2024)
  12. The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro. Wang X, Nyenhuis SB, Bernstein HD. Nat Commun 15 7246 (2024)
  13. YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane of Escherichia coli. Kumar S, Davis RM, Ruiz N. Proc Natl Acad Sci U S A 121 e2321512121 (2024)