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BamB facilitates folding of outer membrane protein A (OmpA) via interactions of its β-propeller with the membrane surface and via a conformation change induced by phosphatidylglycerol
A sufficient folding and insertion of OMPs into the OM of Gram-negative bacteria requires the conserved β-barrel assembly machinery (BAM) complex. The present thesis concerns the structural properties and folding behavior of the lipoprotein BamB and describes its relevance in the synchronized mechanism of membrane insertion and folding of the β-barrel protein OmpA. Furthermore, specific binding sites in BamB involved in the interaction to the lipid membrane or the periplasmic domain of BamA (PD-BamA) were identified ...