Fig. 5
From: Structural and functional insights into the lipopolysaccharide ABC transporter LptB2FG
LptB structure and its interactions with LptF and LptG. a Superimposition of dimeric LptB of K. pneumoniae (blue and green) and that of E. coli (magenta) in complex with ATP (PDB access code 4QC2). The structure of E. coli’s dimeric LptB shifts around 13 Å from the ATP-free structure of the dimeric LptB in the K. pneumoniae LptB2FG. b The conserved residues of the LptB and the coupling helices of LptF and LptG. The most variable residues are in cyan and the most conserved residues are in dark red. The coupling helices of LptF and LptG, between TM2 and TM3, are located at the LptB middle groove. c The residues of coupling helix of LptF and TM1F (cyan) interact with the residues of one LptB monomer (blue). The residues (LptB residues L72, H73, F90, and I105, and LptF V87) that formed the UV-dependent crosslinks are shown in red 41. d The residues of the coupling helix of LptG and TM1G (yellow) interact with residues of another LptB monomer (green). The residues (LptB residues L72, H73, F90, and V102, and LptG S95) that formed the UV-dependent crosslinks are shown in magenta 41
