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Figure 9 | BMC Microbiology

Figure 9

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 9

Model of post-translational regulation of TnaA activity by focus formation. Four TnaA units (magenta, blue, cyan and orange) were modeled as dimers and as the tetramer by using the PISA software, based on the crystal structure PDB 2OQX. Focus assembly of TnaA monomers and dimers would prevent the protein from assembling into active tetramers and/or trap the catalytic pocket in a closed conformation, thus regulating TnaA activity.

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