Fig. 2: TslA has ‘reverse’ LXG architecture but can interact with Lap-like proteins.

a Structural model of TslA obtained from the AlphaFold Database⁷². The N- terminus is indicated. The inset shows the predicted active site. b The LXG-like C-terminus of TslA (maroon) aligned with the S. intermedius LXG protein, TelC (obtained from the AlphaFold Database and shown in gold). The inset depicts the L-X-G motif of TelC (yellow) and the G-X-L motif of TslA (red). c Model of the complex composed of TilA (blue), TslA (maroon), TlaA1 (beige), TlaA2 (pale blue) generated with AlphaFold Colab⁷⁵. The predicted alignment error for the model is provided, with the sequence order being the same as the order listed above. d Size exclusion chromatogram of TslA_CT-TlaA1-TlaA2 containing fractions that had been previously co-purified by Ni-affinity chromatography followed by Streptactin affinity chromatography. This experiment has been performed three times, with similar results observed for each. AU—absorbance units. e SDS PAGE analysis of the indicated peak fractions from (d). f The protein fraction indicated with an asterisk in (e) was analysed by western blotting with anti-TslA, anti-Strep and anti-Myc antibodies, as indicated. This experiment has been performed twice, each with similar results. The uncropped blots from (f) can be found in Supplementary Fig. 10.