Fig. 1: Bap1 and RbmC contain modular and overlapping domains for surface adhesion. | Nature Communications

Fig. 1: Bap1 and RbmC contain modular and overlapping domains for surface adhesion.

From: Vibrio cholerae biofilms use modular adhesins with glycan-targeting and nonspecific surface binding domains for colonization

Fig. 1

a Schematic of Bap1 and RbmC structural domains. Red dots correspond to the positions of the N-glycan binding pockets. b Crystal structure of Bap1 without the 57aa loop and the corresponding cartoon for each domain. The position of the 57aa loop (magenta) and the β-strand from β-propeller blade 1 that contributes to the Velcro closure (red) are indicated. c Schematic and hypothetical functions of domains in Bap1 (Left) and RbmC (Right). d Working model. Both proteins function as “double-sided tape” for V. cholerae biofilms: they share a conserved β-propeller that binds to VPS. Bap1 adheres to lipids and abiotic surfaces primarily via the 57aa loop while RbmC mainly mediates binding to host surfaces via N-glycan-binding pockets in its β-prismCs and the mucin-binding domains M1M2. Created with Biorender.com.

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