Fig. 2 | Signal Transduction and Targeted Therapy

Fig. 2

From: Deciphering the molecular basis of lipoprotein recognition and transport by LolCDE

Fig. 2

Identification of the allosteric communicating residues of NBDs and TMDs of the LolCDE complex. a Cryo-EM density map (left) and cartoon representation (right) of LolCDE171QE structures in nanodiscs with ATP binding at 3.2 Å resolution. LolC and LolE are shown in purple and green, LolD dimer is shown in pink and yellow, and ATP is shown in gray, respectively. b Side and top views of the NBDs showing interactions with the coupling helices of LolC and LolE. The bound endogenic ATP molecules and magnesium ions are indicated. c Cell viability of the LolCDE mutants of the coupling helix interacting residues. Data are representative of n = 3 independent experiments. d Structural superimposition of the coupling helices of LolC (left) and LolE (right) and the NBDs of the lipoprotein-bound and ATP-bound LolCDE structures, showing distinct interactions at the coupling helices between the two structures

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