Fig. 3 | Nature Communications

Fig. 3

From: Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR

Fig. 3

BamAP4P5–BamCDE interface in bilayers. a Close up of representative correlations from the 2D 13C–13C spectra of AVLTI labeled BamAP4P5 in liposomes, in the absence and presence of BamCDE (blue and red spectra, respectively). Crosses are assignments of the labeled residues; dashed boxes indicate correlations with chemical shift perturbations above 0.7 ppm. b BamAP4P5–BamCDE interaction interface as described by ssNMR data in lipid bilayers. Residues as sticks are labeled (i.e. AVLTI), those in gray were not used for analysis. Residues in red show a chemical shift perturbation, those that in yellow indicate an increase in intensity and those that in green do not experience any effect upon complex formation. The zoom-in shows in more detail the interaction interface. Indicated are the structural elements mentioned in the text and residue I668 of EL6 (spheres). c BamA–BamCDE interface as described by all BAM complex crystal structures (PDB 5D0O, 5D0Q, 5AYW, and 5EKQ). Contacts with the BamCDE complex, in red, were found using PDBePISA29 on these structures. BamD and BamE are shown as semi-transparent surfaces in b, c, as well as a schematic representation of the liposome bilayer and detergent micelle are present to aid visualization

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