Extended Data Fig. 5: The BLI results on the interactions between the four TEF30 mutants and PSII-C as well as the interactions between the two domains within TEF30.
a, Constructs of TEF30 mutants indicated with cartoon models. Red parts correspond to the deleted regions of the protein. b, The BLI analysis on the kinetics of the interactions between PSII-C and the TEF30 mutants loaded on sensors. The plots were generated using OriginPro. The colored curves are recorded data, and the black curves are the models fitted with the data. The PSII-C concentrations are labeled in the top right corner of the plots. The calculated dissociation constants and R-squared values are labeled below the curves. c, The response signals generated by the interactions of 125 nM PSII-C with the TEF30-immobilized sensors. TEF30-WT–LHCII was included as a negative control, providing the signals from the barely detectable interaction of TEF30-WT with 125 nM LHCII trimer. d, The polar interactions between the H0 helix of PDZ domain and the H3 and H5 helices of TPR domain in TEF30. The amino acid residues involved in the interactions were shown as sticks. The distances (Å) between the two adjacent groups are labeled nearby the dash lines. e, The cryo-EM density and structure model of TEF30 in TEF30-C. The PDZ domain (Pro78-Tyr154) and the TPR domain (Tyr181-Lys320) is colored in lime green and warm pink respectively.
