fig3

Figure 3. Molecular modeling and comparison of select classical and evolved Dit proteins. Structural alignment of the AlphaFold predicted Dit models for phages D2929 (green) and M7361 (blue), respectively (image A). The region corresponding to the insert present in D2929 is shown on the left-hand side of the figure, with the locations of the three predicted carbohydrate-binding regions (two of them corresponding to the proximal domain and one corresponding to the distal domain) highlighted in different colors. Structural alignment of the D2929 (green) and D6887 (blue) Dit models is provided in panel B on the right-hand side of the figure with an alignment corresponding only to the insert regions provided in panel C at the bottom. The predicted carbohydrate-binding motif in D6887 is highlighted in yellow. Panel D at the bottom right shows a structural alignment of the D4006 Dit protein predicted to possess BppA domains aligned with the minor structural protein 5 (BppA) from the TUC2009 solved baseplate structure (PDB: 5E7T). It can be clearly seen in the proximal portion of the insert in D4006 that there is a structural similarity with BppA. BppA: accessory base plate protein; Dit: distal tail protein; PDB: protein data bank.