Figure 3 | Scientific Reports

Figure 3

From: Substrate size-dependent conformational changes of bacterial pectin-binding protein crucial for chemotaxis and assimilation

Figure 3

Conformational changes of SPH1118. (a) N terminal domains of ligand-free and -bound SPH1118 were superimposed. The right structure is rotated 90° toward the reader relative to the left one. Blue, SPH1118 (full open form); green, SPH1118 (open form); red, SPH1118 (closed form); cyan, SPH1118/GalUA; magenta, SPH1118/2 × MES; orange, SPH1118/ΔtriGalUA. Ribbon models show the main chains of SPH1118. (–) represents the direction in which the C terminal domain closes. Compared with the C terminal domain of SPH1118 (full open form), those of SPH1118 (open form), SPH1118 (closed form), SPH1118/GalUA, SPH1118/2 × MES, and SPH1118/ΔtriGalUA were closed by 18.9°, 34.2°, 38.1°, 40.3°, and 43.4°, respectively. (b) N terminal domains of ligand-bound SPH1118 were superimposed. The right structure is rotated 90° toward the reader relative to the left one. Ribbon and ball models show the main chain of SPH1118 and each ligand (GalUA, MES, and ΔtriGalUA), respectively. Cyan, SPH1118/GalUA; magenta, SPH1118/2 × MES; orange, SPH1118/ΔtriGalUA.

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