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Fig. 2 | BMC Microbiology

Fig. 2

From: Flagellin, a plant-defense-activating protein identified from Xanthomonas axonopodis pv. Dieffenbachiae invokes defense response in tobacco

Fig. 2

Molecular docking analysis of Xad1Flg22(orange) with FLS2 (violet) and BAK1 (wheat) complex. (A) The Flg22Xad1 peptide regions, when docked with the FLS2-BAK1 complex, revealed Flg22Xad1 binds to a shallow groove at the inner surface of the FLS2-LRR as found in the crystal structure of the solved Flg22-FLS2-BAK1 complex (PDB: 4MN8). (B) The superimposition of the docked complex (Flg22Xad1-FLS2-BAK1 in orange-violet-wheat) with the crystal structure 4MN8 (Flg22-FLS2-BAK1 in green-pink-blue) had similar folding and positioning in the structure alignment (C) The Flg22Xad1 (yellow) interacted with the FLS2 (blue) spanning LRR 6–17. (D) The interaction of Flg22Xad1(yellow) with FLS2 (blue) was stabilized through H-bonding (yellow dash) and hydrophobic interaction

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BMC Microbiology

ISSN: 1471-2180

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