Fig. 2: Structure of the α-domain of Ag43EDL_933 (α43_EDL933), Ag43UTI89 (α43_UTI89), and Ag43b (α43b). | npj Biofilms and Microbiomes

Fig. 2: Structure of the α-domain of Ag43EDL_93343_EDL933), Ag43UTI8943_UTI89), and Ag43b (α43b).

From: Variation of Antigen 43 self-association modulates bacterial compacting within aggregates and biofilms

Fig. 2: Structure of the α-domain of Ag43EDL_933 (α43_EDL933), Ag43UTI89 (α43_UTI89), and Ag43b (α43b).The alternative text for this image may have been generated using AI.

a, b Side and top cartoon representations with β-strands in green, purple and blue, respectively. Turns are coloured in salmon and F1–F3 represent the three faces of the three-stranded β-helix. The two loops (loop 1 and loop 2) that protrude from the β-helices are shown in black, while the four β-hairpins appear in light orange. The AC domain of both α43_EDL933 and α43_UTI89 are coloured in hot pink. Side view of α43a (PDB: 4KH3), depicted in grey is shown for comparison13. c Stereo view of the 2Fo−Fc electron density maps contoured at 1σ of a cross-section of α43_EDL933 (residues T65-D84), α43_UTI89 (residues L90-E108) and α43b (residues I52-D70) β-helices. d Superimposition of α43_EDL933, α43_UTI89 and α43b on that of α43a, with α43a depicted in grey. The AC domain is displayed in hot pink and light pink for α43_EDL933 and α43_UTI89 respectively, with the β-hairpin motifs yellow. RMSD values for all superpositions are shown in Supplementary Table S1.

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