Figure 6
From: Structural insights into phosphatidylethanolamine formation in bacterial membrane biogenesis
Key residues required for auto-cleavage of proenzyme. (A) Putative active site for auto-cleavage is shown where amino acid residues selected for mutagenesis are highlighted as sticks (Left). Wild-type and site-specific mutant proteins are visualized by immunoblot from cell lysates after 4 h induction (Top Right), and the purified recombinant proteins are analyzed by Coomassie staining on 12% SDS-PAGE gel (Bottom Right). Proenzyme (theoretical molecular weight, 36.9 kDa), processed β-chain (28.6 kDa), and α-chain (8.3 kDa). Lane M ladder marker. (B) LC–MS analysis of PS decarboxylation activity of Asp-90 mutants. Mean and standard deviation are plotted. Experiments were performed in triplicates.
