Fig. 5
From: Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR
Structure and dynamics of BamAP4P5 are influenced by complex formation. a Dynamic BamAP4P5 protein region (indicated in red) as judged from ssNMR (1H-detected and DNP) experiments in proteoliposomes. In blue are residues which show no significant changes upon complex formation. In black are residues that could not be assigned by ssNMR CαNH and CONH experiments. b Conformational changes within BamAP4P5 upon complex formation with the sub-complex BamCDE. Inset at left is the movement of P5 to beneath the β-barrel, indicated by the red arrow, a movement that is anchored in place by residues from periplasmic loop 4 and residue F394 (red), which exhibits chemical shift perturbation in ssNMR experiments. Inset at right top, the EL6 loop anchored to the barrel via the conserved VRGF motif, which exhibits no changes as judged by the proximal I668. Inset right bottom: distance measurement between I806 and F428 that allows to follow lateral gate opening occurring upon complex formation
