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. 2020 Dec 10;3:752. doi: 10.1038/s42003-020-01492-1

Fig. 4. Substrate-binding destabilized the hydrophobic cluster in LRR-CT.

Fig. 4

A Left, superimposition of the structures of IpaH9.8LRR-Sub, IpaH9.8LRR-Sub’ (PDBID: 6K2D), IpaH9.8LRR-FL, and IpaH9.8LRR-iso (PDBID: 5B0T) by the LRR-NT with the LRR domains differentiated by colors. Arrows indicate the rotation of LRR-CT when bound to hGBP1. Right-top and right-bottom, magnified view of LRR-CTs in different IpaH9.8LRR constructs as in left. Relative differences in shift distance (top) and rotation angles (bottom) for LRR-CT are indicated. B The cartoon models of IpaH9.8LRR-Sub, IpaH9.8LRR-Sub’, IpaH9.8LRR-FL, and IpaH9.8LRR-iso are colored by normalized B-factor (1 to 0 to −1; red to white to blue, red indicating flexibility and white indicating stability).