Extended Data Fig. 6: Comparison of B. thetaiotaomicron and E. coli BamA β-barrels.
From: Structure of a distinct β-barrel assembly machinery complex in the Bacteroidota
a, Structure-based sequence alignment of BtBamA and E. coli BamA (EcBamA). Sequence identity – 22%, TM-align score – 0.64. The β-barrel strands of BtBamA and EcBamA are annotated, respectively, above and below the sequence alignment. Extracellular loops (EL) of interest are annotated. b, c, AF2 models of BtBamA (b) and EcBamA (c) β-barrels with extracellular loops coloured as in (a). d, The position of the tyrosine-rich loop (EL 3) in the context of the whole BtBAM complex. The AF2 model of BtBamA, coloured as in b, is superposed on the experimental BtBamA structure. No cryo-EM density for the tyrosine-rich loop was observed. Inset 1 shows a close-up view of EL3 inside the dome. Inset 2 shows the same view of BtBamA as inset 1 with the other BAM components omitted for clarity. e, WebLogo92 representation of the Bacteroidota BamA EL3 region generated from 861 aligned BlastP hits shows enrichment of tyrosine, glycine and asparagine residues.
