Protein oligomerization in the bacterial outer membrane (Review)

Figures & data

Figure 1.  Protein oligomerization in the bacterial outer membrane. Top and side views of the oligomerization topologies observed in known outer membrane protein structures. OM single pores: (A) Trimeric β-barrels: Hia (left, PDB code: 2GR7) and TolC (right, PDB code: 1EK9) (B) Multimeric superchannels: PulD secretin, obtained from [83] and (C) α-helical barrels: Wza (2J58). OM multipores: (D) Twinned pore oligomers: PapC (PDB code: 2VQI). (E) Triplet pores: LamB (PDB code: 1MAL). All the structures presented in this figure are scaled against the estimated width of outer membrane bilayer (36 Å). Figure is prepared using pymol [84].

Figure 2.  Functional significance of protein oligomerization in the bacterial outer membrane. (A) Model for the TolC-AcrA-AcrB acridine efflux pump [85]. The three monomers in TolC, AcrA and AcrB trimers are colored yellow, magenta and cyan, red, orange, maroon, slate, greencyan. (B) Model of three-subunit assembly intermediate of the type 1 pilus bound to the FimD usher twinned pore [50]. The twinned pores are shown in yellow and magenta, with the FimH, FimG and FimF subunits and FimC chaperone shown in skyblue, cyan, blue, and green, respectively. The model includes a newly recruited chaperone subunit complex (FimC:FimA in green:dark blue) bound to the N-terminal domain of the second usher pore/monomer. Figure is prepared using pymol.

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