@article{198961,
  keywords = {Models, Molecular, Protein Structure, Tertiary, Humans, Membrane Proteins, Cell Membrane, Multiprotein Complexes, Protein Folding, Protein Structure, Secondary, Molecular Chaperones, Protein Transport, Bacterial Outer Membrane Proteins},
  author = {Christine Hagan and Thomas Silhavy and Daniel Kahne},
  title = {β-Barrel membrane protein assembly by the Bam complex},
  abstract = { β-barrel membrane proteins perform important functions in the outer membranes (OMs) of Gram-negative bacteria and of the mitochondria and chloroplasts of eukaryotes. The protein complexes that assemble these proteins in their respective membranes have been identified and shown to contain a component that has been conserved from bacteria to humans. β-barrel proteins are handled differently from α-helical membrane proteins in the cell in order to efficiently transport them to their final locations in unfolded but folding-competent states. The mechanism by which the assembly complex then binds, folds, and inserts β-barrels into the membrane is not well understood, but recent structural, biochemical, and genetic studies have begun to elucidate elements of how the complex provides a facilitated pathway for β-barrel assembly. Ultimately, studies of the mechanism of β-barrel assembly and comparison to the better-understood process of α-helical membrane protein assembly will reveal whether there are general principles that guide the folding and insertion of all membrane proteins. },
  year = {2011},
  journal = {Annu Rev Biochem},
  volume = {80},
  pages = {189-210},
  issn = {1545-4509},
  doi = {10.1146/annurev-biochem-061408-144611},
  language = {eng},
}