title: Membrane protein architects: the role of the BAM complex in outer membrane protein assembly.
abstract: The folding of transmembrane proteins into the outer membrane presents formidable challenges to Gram-negative bacteria. These proteins must migrate from the cytoplasm, through the inner membrane and into the periplasm, before being recognized by the beta-barrel assembly machinery, which mediates efficient insertion of folded beta-barrels into the outer membrane. Recent discoveries of component structures and accessory interactions of this complex are yielding insights into how cells fold membrane proteins. Here, we discuss how these structures illuminate the mechanisms responsible for the biogenesis of outer membrane proteins.
authors.affiliation: Cancer Research UK Institute for Cancer Studies, School of Cancer Sciences, Edgbaston, Birmingham, UK.
authors.forename: Timothy J
authors.initials: TJ
authors.lastname: Knowles
authors.forename: Anthony
authors.initials: A
authors.lastname: Scott-Tucker
authors.forename: Michael
authors.initials: M
authors.lastname: Overduin
authors.forename: Ian R
authors.initials: IR
authors.lastname: Henderson
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D006090:Gram-Negative Bacteria / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism; D017510:Protein Folding; D055503:Protein Multimerization; D021381:Protein Transport
chemical_list: D001425:Bacterial Outer Membrane Proteins; C503914:BamA protein, E coli; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones