Fig. 4
Molybdenum-binding proteins are enriched in antioxidative properties in strains with both high and low predicted levels of endogenous ROS as well as strain pathotypes likely encountering oxidative environments. a PCA of antioxidative properties for molybdenum-binding proteins of strains, in relation to their predicted ROStype and annotated pathotype. Proteins were inspected individually for changes in antioxidative properties, since analysis of the component contributions showed both enrichment and avoidance of certain properties. b Biotin sulfoxide reductase shows avoidance of surface-exposed cysteine residues in both ROShi/ROSlo and ExPEC/AIEC/APEC strains. The residues highlighted on the protein structure indicate common mutations in strains of ExPEC/AIEC/APEC pathotypes. The size of the highlighted residue corresponds to the number of strains that mutation appears in. Note that all mutations do not co-occur together in all strains. The distribution plots for strain phenotypes to the right of the protein figure show the normalized percentage of the residue in relation to the protein subsequence, i.e. percentage of cysteines on the protein surface. c Xanthine dehydrogenase subunit A similarly shows enrichment of antioxidative properties, by avoiding carbonylatable and charged residues on the protein surface, along with an increase of a total percentage of order-promoting residues. Structural models shown here are all homology models from the SWISS-MODEL database [48]