Fig. 5: AlphaFold-Multimer generated model of the BAM–SurA complex. | Communications Biology

Fig. 5: AlphaFold-Multimer generated model of the BAM–SurA complex.

From: Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding

Fig. 5

a, b The predicted structure of the BAM–SurA complex coloured by subunit. SurA is in grey. c, d Surface views of the BAM–SurA complex with regions of HDX protection in the BAM complex upon binding SurA highlighted, and SurA coloured by domain. Regions of BAM that are protected from HDX in the presence of SurA are highlighted in blue. Regions in white show no change in deuterium uptake in the presence of SurA, while those in dark grey denote sequences for which peptides were not detected. Patches of protection from HDX upon SurA binding in the BamA β-barrel domain (adjacent to the lateral gate), POTRAs 1 and 2, BamB, and BamE/POTRA 4 are ringed in magenta. The SurA core, P1 and P2 domains are coloured in orange, green and yellow, respectively. Left panels show a side view of the complex, and right panels a view from the periplasmic face.

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