title: Identification of BamC on the Surface of E. coli.
abstract: In order to relate the structural architecture of the BAM complex to its function in outer membrane protein assembly, the arrangement of each component within the complex is vital. This chapter explores the structure and topology of BamC, using a range of biochemical techniques to probe the topology and surface exposure.
authors.affiliation: Department of Microbiology, Monash University, Building 77, 23 Innovation Walk, Clayton Campus, Melbourne, VIC, 3800, Australia. chaille.webb@monash.edu.
authors.forename: Chaille T
authors.initials: CT
authors.lastname: Webb
authors.affiliation: Department of Microbiology, Monash University, Building 77, 23 Innovation Walk, Clayton Campus, Melbourne, VIC, 3800, Australia. trevor.lithgow@monash.edu.
authors.forename: Trevor
authors.initials: T
authors.lastname: Lithgow
mesh_terms: D000818:Animals; D004797:Enzyme-Linked Immunosorbent Assay; D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000302:isolation & purification / Q000378:metabolism*; D047468:Immunoprecipitation; D058635:Lipid-Linked Proteins / Q000302:isolation & purification / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D010447:Peptide Hydrolases / Q000378:metabolism
chemical_list: C556681:BamC protein, E coli; D029968:Escherichia coli Proteins; D058635:Lipid-Linked Proteins; D010447:Peptide Hydrolases
keywords: Immunofluorescence; Lipoprotein; Outer membrane; Surface exposure; Topology