Skip to main content
Figure 2 | BMC Microbiology

Figure 2

From: A new suite of tnaA mutants suggests that Escherichia coli tryptophanase is regulated by intracellular sequestration and by occlusion of its active site

Figure 2

Construction of TnaA truncation mutants. The regions of the D1, D2 and D3 subdomains were determined according to the TnaA crystal structure (PDB 2OQX). The position of the active site Lys270 is indicated. In D2, D3 and D2D3, the starting methionine codon was retained. In D1D3, a short linker (Ala-Ala-Gly-Tyr-Asp) was inserted between the two subdomains. All proteins were constructed to contain a C-terminal sfGFP. Each gene was inserted into the chromosome to replace the wild type tnaA gene at that position.

Back to article page