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. 2008 Jul 22;105(30):10348–10353. doi: 10.1073/pnas.0803039105

Fig. 2.

Fig. 2.

The overall fold of H. pylori MotB-C and comparisons with other OmpA-like PG-binding domains. (A) Stereo representation of the MotB-C structure. The bound NAM molecule is shown in stick mode. The figure was prepared by using PyMOL (20). (B) Comparison of the structures (Upper) and the secondary structure topologies (Lower) of MotB-C from H. pylori, the periplasmic domains of PALs from E. coli and H. influenzae, and the PG-binding domain of RmpM from N. meningitidis. The conserved structural core is drawn in black and white in the topology schemes and colored cyan/magenta (helices/strands) in the 3D structure representation. Topological differences are highlighted with distinct colors. (C) Sequence alignment of the C-terminal domains of MotBs from H. pylori and E. coli and the OmpA-like domains shown in B. Conserved residues are highlighted in red. The positions of the aa substitutions associated with loss of function in E. coli MotB (11) are shown by black dots. Alignment was carried out by using the ClustalW server (25) and further refined based on structure superpositions. The figure was produced by using ESPript (26). (D) Stereoview of the superposition of the structures of MotB-C (blue), the periplasmic domains of PALs from E. coli (red), and H. influenzae (green) and the PG-binding domain of RmpM from N. meningitides (magenta). The 10 conserved residues are shown in black in the MotB-C structure.