Fig. 3: The cryo-EM structure of human RNF213 with IpaH1.4. | Nature Communications

Fig. 3: The cryo-EM structure of human RNF213 with IpaH1.4.

From: Shigella effector IpaH1.4 subverts host E3 ligase RNF213 to evade antibacterial immunity

Fig. 3

a A schematic diagram showing the domain organizations of human RNF213 and S. flexneri IpaH1.4. In this drawing, the interaction between these two proteins is indicated by a two-way red arrow, and the domain boundaries of RNF213 are further labeled. The color scheme for domains of RNF213 and IpaH1.4 presented in this panel is used throughout all figures. b The front and side views of the cryo-EM map of human RNF213. c The front and side views of the cryo-EM structure of human RNF213 with the same orientation and color scheme as in (b). d The local refined cryo-EM map of the E3 module region of RNF213 with clear additional density (yellow) around the RING domain of RNF213, which is partially matched with the IpaH1.4 LRR domain. e The fitted structure model of RNF213 E3 module in complex with IpaH1.4 LRR based on the local refined cryo-EM map in (d).

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