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Fig. 5 | Phytopathology Research

Fig. 5

From: Crystal structure of rice APIP6 reveals a new dimerization mode of RING-type E3 ligases that facilities the construction of its working model

Fig. 5

Identification of AvrPiz-t interaction region(s) on APIP6 and a working model of APIP6. a Identification of the AvrPiz-t interaction region(s) on APIP6 with Y2H. Truncates of APIP6 were designed according to prediction of secondary structures. Truncates that could or could not interact with AvrPiz-t are colored green or orange, respectively. b A working model of APIP6 with ubiquitin-conjugated E2. The position of E2 and ubiquitin were determined by structural superimposition with the complex structure of RNF4/UBCH5A/Ub (PDB accession number 4AP4). The N-terminal and C-terminal regions of the RING motif of APIP6 are denoted as blue or red flexible lines. The two regions of APIP6, i.e. Pro120–Glu140 and Phe219–Gln254 that are responsible for AvrPiz-t interaction, are labeled. The determined solution structure of AvrPiz-t (PDB accession number 2LW6) was used to show the possible position of AvrPiz-t in the E2/APIP6/Ub complex model. The lysine residues on the surface of AvrPiz-t, which are probably to be conjugated to ubiquitin, are shown as pink

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Phytopathology Research

ISSN: 2524-4167