title: The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of β-barrel assembly.
abstract: β-Barrel proteins are folded and inserted into the outer membranes of Escherichia coli by the Bam complex. The Bam complex has been purified and functionally reconstituted in vitro. We report conditions for reconstitution that increase the folding yield 10-fold and allow us to monitor the time course of folding directly. We use these conditions to analyze the effect of a mutation in the Bam complex and to demonstrate the ability of the reconstituted complex to catalyze more than one round of substrate assembly.
authors.affiliation: Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, United States.
authors.forename: Christine L
authors.initials: CL
authors.lastname: Hagan
authors.forename: Daniel
authors.initials: D
authors.lastname: Kahne
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics* / Q000502:physiology; D002384:Catalysis; D020134:Catalytic Domain / Q000235:genetics; D004926:Escherichia coli / Q000737:chemistry* / Q000235:genetics*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics* / Q000502:physiology; D016297:Mutagenesis, Site-Directed; D011485:Protein Binding / Q000235:genetics; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary / Q000235:genetics; D013379:Substrate Specificity / Q000235:genetics
chemical_list: D001425:Bacterial Outer Membrane Proteins; C503914:BamA protein, E coli; D029968:Escherichia coli Proteins