Predicting functionally informative mutations in Escherichia coli BamA using evolutionary covariance analysis.

ABSTRACT: The essential outer membrane β-barrel protein BamA forms a complex with four lipoprotein partners BamBCDE that assembles β-barrel proteins into the outer membrane of Escherichia coli. Detailed genetic studies have shown that BamA cycles through multiple conformations during substrate assembly, suggesting that a complex network of residues may be involved in coordinating conformational changes and lipoprotein partner function. While genetic analysis of BamA has been informative, it has also been slow in the absence of a straightforward selection for mutants. Here we take a bioinformatic approach to identify candidate residues for mutagenesis using direct coupling analysis. Starting with the BamA paralog FhaC, we show that direct coupling analysis works well for large β-barrel proteins, iden

SUBMITTER: Dwyer RS 

PROVIDER: S-EPMC3781972 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature