FIGURE 1.

Sequence alignment of LolB homologues and positions of mutated residues. A, the amino acid sequences of LolB and its homologues were aligned using ClustalW (26). Residues forming α and 3¹⁰ helices and β-strands are indicated. Conserved residues that were subjected to random mutagenesis are indicated in red with their position numbers. Eco, E. coli; Sty, Salmonella enterica serovar typhimurium; Ype, Yersinia pestis; Hin, Haemophilus influenzae; Aac, Actinobacillus actinomycetemcomitans; Pmu, Pasteurella multocida. B, the positions of mutated residues are shown in the structure of mLolB. Side chains of the residues are shown as sticks, whereas C_α atoms of glycine are shown as spheres. C, mLolB is represented as a ribbon model in which strands and helices are colored cyan and red, respectively. The side chain of Leu-68 in the hydrophobic loop is shown as a CPK model in green.