FIGURE 8.

AlphaFold and ColabFold structure predictions of the LnsAB complex. (A) AlphaFold model of LnsA from S. aureus. The cartoon is colored in a rainbow based on the confidence, where red is low and violet is high confidence. The first ∼ 40 residues are modeled with low confidence and are not reliable (large unstructured yellow and orange tail). (B) ColabFold model of the LnsAB complex. On the left, the full LnsA sequence was used to model the complex. LnsA is colored red and LnsB green. On the right, the first 27 amino acids were deleted, mimicking the case where the predicted signal peptide in LnsA has been cleaved off by signal peptidase I. LnsA is colored in deep red and LnsB in teal. (C) Structure of the nitrilase-like domain in Lnt from E. coli (left) and the core domain of LnsA (right). Helices are colored green, β-sheets blue and unstructured regions orange. Components of the αββα sandwich fold in Lnt and the simplified αβα fold in LnsA are indicated. (D) View of the proposed catalytic residues. His60, Gln72, Glu74, and Cys143 are shown as sticks colored by element with magenta for carbon, blue for nitrogen, yellow for sulfur and red for oxygen. The distance between His60 and Cys143 is indicated.