Fig. 5: A conserved electrostatic surface in the C-terminal lobe of Tap14 recognizes the b-cage domain of RhsP2. | Nature Communications

Fig. 5: A conserved electrostatic surface in the C-terminal lobe of Tap14 recognizes the b-cage domain of RhsP2.

From: A widespread accessory protein family diversifies the effector repertoire of the type VI secretion system spike

Fig. 5

A AlphaFold3 prediction of the complex formed between RhsP2Cage and Tap14. B Western blot analysis of co-purification experiments between the indicated heterologously expressed tagged (hexahistidine (H) or FLAG (F)) proteins. RhsP2 was detected using a polyclonal antibody raised against a truncation of this protein lacking its C-terminal toxin domain. C Molecular contacts present at the predicted interface between RhsP2Cage and Tap14. D Western blot analysis of co-purification experiments between the indicated heterologously expressed tagged (hexahistidine (H) or FLAG (F)) proteins. E Electrostatic surface representation of the indicated proteins. Dashed line indicates surface contacting RhsP2Cage in the AlphaFold3 model depicted in B. Color corresponds to charge as indicated by the scale bar. Western blots are representative of three independent experiments.

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