Figure 5 | Scientific Reports

Figure 5

From: Alternative substrate-bound conformation of bacterial solute-binding protein involved in the import of mammalian host glycosaminoglycans

Figure 5

Hinge-bending motion of substrate-free and substrate-bound Smon0123. (A) N domains of substrate-free and substrate-bound Smon0123 were superimposed. Gray, CΔ0S-bound; green, CΔ4S-bound; blue, CΔ6S-bound; pink, CΔ4S6S-bound; and olive, substrate-free Smon0123. Ribbon models and ball models show the main chain of Smon0123 and disaccharides, respectively. Although the domains of CΔ0S-, CΔ4S-, and CΔ6S-bound Smon0123 were 47° more closed than those of substrate-free Smon0123 (left), the hinge-bending motion of CΔ4S6S-bound Smon0123 was 39° (right). (B) Smon0123 amino acid residues directly formed hydrogen bonds with CΔ0S (gray), CΔ4S (green), CΔ6S (blue), and CΔ4S6S (pink). (C) Some residues of CΔ4S6S-bound Smon0123 (pink) located in a different position from those in the other substrate-bound Smon0123 (gray, CΔ0S; green, CΔ4S; and blue, CΔ6S). The stick models show unsaturated chondroitin disaccharides, and the line models show Arg204, Lys210, Trp284, and Ser287 residues. Small cyan balls show water molecules (oxygen atoms). Magenta and cyan dashed lines show direct and indirect hydrogen bonds, respectively.

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