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Fig. 1 | Phytopathology Research

Fig. 1

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. 1

Crystal structure of APIP6-RING exhibits a novel dimerization mode of RING-type E3s. a A diagram of APIP6 and its truncates. Protein crystal was only obtained with the 33–92 truncate. b Overall structure of the APIP6-RING homodimer. The two chains are colored chartreuse or light orange, respectively. The coordination residues to zinc ions are shown as sticks on the side view of the protein structure. c A representative homodimer of RING-type E3 (PDB accession number 2YHO), showing the dimer mode is different from APIP6-RING. The ring motif of the two molecules are colored pink and cyan, respectively, and the other regions are colored wheat. In b, c, zinc ions are shown as grey spheres. d Recombinant APIP6-RING protein mainly exists as homodimer in solution as evaluated by the SV-AUC method. Mf: calculated molecular weight of the corresponding fraction. e APIP6-RING protein forms homodimer as evaluated by Y2H assay. f APIP6-RING also forms dimer in vivo as shown by LCI assay

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Phytopathology Research

ISSN: 2524-4167