title: Structure and function of BamE within the outer membrane and the β-barrel assembly machine.
abstract: Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential β-barrel assembly machine (Bam). Here, we report the native structure and mechanism of a core component of this complex, BamE, and show that it is exclusively monomeric in its native environment of the periplasm, but is able to adopt a distinct dimeric conformation in the cytoplasm. BamE is shown to bind specifically to phosphatidylglycerol, and comprehensive mutagenesis and interaction studies have mapped key determinants for complex binding, outer membrane integrity and cell viability, as well as revealing the role of BamE within the Bam complex.
authors.affiliation: School of Cancer Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
authors.forename: Timothy J
authors.initials: TJ
authors.lastname: Knowles
authors.forename: Douglas F
authors.initials: DF
authors.lastname: Browning
authors.forename: Mark
authors.initials: M
authors.lastname: Jeeves
authors.forename: Riyaz
authors.initials: R
authors.lastname: Maderbocus
authors.forename: Sandya
authors.initials: S
authors.lastname: Rajesh
authors.forename: Pooja
authors.initials: P
authors.lastname: Sridhar
authors.forename: Eleni
authors.initials: E
authors.lastname: Manoli
authors.forename: Danielle
authors.initials: D
authors.lastname: Emery
authors.forename: Ulf
authors.initials: U
authors.lastname: Sommer
authors.forename: Ashley
authors.initials: A
authors.lastname: Spencer
authors.forename: Denisse L
authors.initials: DL
authors.lastname: Leyton
authors.forename: Derrick
authors.initials: D
authors.lastname: Squire
authors.forename: Roy R
authors.initials: RR
authors.lastname: Chaudhuri
authors.forename: Mark R
authors.initials: MR
authors.lastname: Viant
authors.forename: Adam F
authors.initials: AF
authors.lastname: Cunningham
authors.forename: Ian R
authors.initials: IR
authors.lastname: Henderson
authors.forename: Michael
authors.initials: M
authors.lastname: Overduin
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics; D001665:Binding Sites; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics; D009682:Magnetic Resonance Spectroscopy; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000737:chemistry* / Q000235:genetics; D033903:Periplasmic Proteins / Q000737:chemistry / Q000235:genetics; D010715:Phosphatidylglycerols / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
chemical_list: D001425:Bacterial Outer Membrane Proteins; C513739:BamD protein, E coli; C523551:BamE protein, E coli; D029968:Escherichia coli Proteins; D050505:Mutant Proteins; D033903:Periplasmic Proteins; D010715:Phosphatidylglycerols; D011994:Recombinant Proteins