Fig. 6: The T434A mutation and the LVPR insertion in the hinge region alter BamA conformational dynamics. | Nature Communications

Fig. 6: The T434A mutation and the LVPR insertion in the hinge region alter BamA conformational dynamics.

From: Molecular insights into how the motions of the β-barrel and POTRA domains of BamA are coupled for efficient function

Fig. 6

a Structure of BAM in a lateral-open conformation (PDB 5LJO21) with each subunit coloured. b, c BAM structures showing regions of HDX protection and deprotection in the BAM complex in the presence of the b T434A mutation or c LVPR insertion. Regions protected or deprotected from hydrogen exchange in the mutant complexes are highlighted in blue or red, respectively. Regions in white show no change in deuterium uptake, while those in black denote sequences for which peptides were not detected. Sequence coverage maps are shown in Supplementary Fig. 9, and Wood’s plots are shown in Supplementary Figs. 10–14.

Back to article page