Unknown

Dataset Information

0

The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of ?-barrel assembly.


ABSTRACT: ?-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.

SUBMITTER: Hagan CL 

PROVIDER: S-EPMC3192448 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of β-barrel assembly.

Hagan Christine L CL   Kahne Daniel D  

Biochemistry 20110811 35


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 sub  ...[more]

Similar Datasets

| S-EPMC8620860 | biostudies-literature
| S-EPMC4936103 | biostudies-literature
| S-EPMC3295296 | biostudies-literature
| S-EPMC7918090 | biostudies-literature
| S-EPMC5582053 | biostudies-literature
| S-EPMC8608283 | biostudies-literature
| S-EPMC5889671 | biostudies-literature
| S-EPMC6287456 | biostudies-literature
| S-EPMC2975826 | biostudies-literature
| S-EPMC3780861 | biostudies-other