Fig. 2 | Nature Communications

Fig. 2

From: Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system

Fig. 2

Structural properties of the export gate protein FlhAC. a Cartoon rendering of the crystal structure of FlhAC determined at 1.9 Å resolution. The protein is colored using a continuous-gradient color scheme from the N terminus (blue) to the C terminus (red). b Solvent-exposed surface rendering of FlhAC displayed in the YRB color scheme59 (yellow, carbons not attached to nitrogen or oxygen; red, negatively charged; blue, positively charged). c The FlhAC site determined by NMR to interact with its binding partners is highlighted in pink. d Sequence conservation of FlhAC colored according to residue identity conservation scores obtained by ConSurf60. The binding site is the most conserved surface in FlhAC

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