Fig. 6

R292 of LptF and R301 of LptG are involved in AMP-PNP binding. a A close view of AMP-PNP binding residues with dimeric LptB and R292 of LptF. b A close view of AMP-PNP binding residues with dimeric LptB and R301 of LptG. AMP-PNP molecules are shown in stick, and the cryo-EM map for AMP-PNP are shown in red mesh. c The two cryo-EM structures are superimposed. The arginine residue R292 located on the cytoplasmic loop 2 of LptF shifts around 9.8 Å to interact with AMP-PNP. d The arginine R301 located on the cytoplasmic loop 2 of LptG shifts around 9.1 Å to interact with the AMP-PNP. AMP-PNP molecules are shown in stick, the colour scheme of sfLptB₂FGC AMP-PNP bound is the same as in Fig. 4, and sfLptB₂FG LPS bound is coloured in blue. e Functional assays of the single mutants R292 of LptF and R301 of LptG. NR1113 cells were transformed with empty vector (pTRC99a_Kan, the negative control) or the vector encoding LptB₂F(Flag)G(Myc)C (the positive control). f Detection of protein expression levels of mutants by western blotting. Empty vector (pTRC99a_Kan, the negative control) or the vector encoding LptB₂F(Flag)G(Myc) (the positive control). The bacterial cells for western blotting were cultured in the presence of 0.2% l-arabinose. All results have been confirmed at least three times. Source data are provided as a Source Data file 6f