Extended Data Figure 2: Superimposition of the two BamACDE complexes in the asymmetric unit.
From: Structural basis of outer membrane protein insertion by the BAM complex
The BamACDE complex with the full-length BamC, showing BamA (red), BamC (blue), BamD (magenta) and BamE (cyan). Only N-terminal loop of BamC was observed in another BamACDE complex in the asymmetric unit cell (yellow). The structure data suggests that the role of BamC is to retain the ring structure of BamA and BamD during OMP insertion. a, Membrane view of the superimposed BamACDE complexes. The primary difference is one complex has a complete BamC subunit, which binds BamD, BamE, POTRA 1 and 2, while the second complex only the N-terminal coil structure up to Pro88 is observed and the rest of BamC is disordered. The overall structures of the two complexes are very similar with some conformational changes in the β-strands of barrel and extracellular loops with r.m.s.d. of 0.908 Å over 378 Cα atoms, while the periplasmic circular structure has some rotation (see arrows) with a r.m.s.d. of 4.706 Å over 385 Cα atoms. b, Periplasmic view of the superimposition of the two structures. The periplasmic circular structure has some rotations when the C-terminal global ___domain binds on the POTRA 2. c, Superimposition of the barrels of the two complexes. d, Superimposition of the two BamCs. The N-terminal coil structures superimpose well with a r.m.s.d. of 0.807 Å over 86 Cα atoms.
