Figure 4

DraB as a model of the FGL subfamily of chaperones. (A) Characteristic elements of the DraB structure (PDB ID: 4DJM) specific to the FGL chaperones in relation to the PapD (PDB ID: 2WMP), - the representative of the FGS subfamily. The part of β-strand A1 with hydrophobic residues participating in subunit interaction represented in the bonds mode is denoted in red. The fragment of the long N-terminal region of the β-strand A1 characteristic for FGL chaperones observed in the DraB is denoted in yellow. The F1 strand-loop-G1 strand hairpin motif is denoted in green with the alternating hydrophobic residues of the β-strand G1 participating in the DSC reaction denoted in the bonds mode. In the F1-G1 loop of the DraB protein, the conserved residue motif KDW characteristic for FGL chaperones are marked with the bond mode. The disulfide bond binding β-strands F1 and G1 in the DraB structure conserved in the entire FGL subfamily is marked in yellow bond mode. The F1-G1 loop region was modeled using MODELLER v9.2 software. (B) Structural alignment of the usher binding site of DraB (red) and PapD-pilicide (PDB ID: 2J7L) (blue) with denoted hydrophobic patch that includes I93, L32, V56 (PapD) and I110, L56, L32 (DraB) residues forming pilicide (pink) binding motif. At the beginning of the F1-G1 loop the region of two proline residues forming “proline lock” conserved in the family of chaperones is denoted (P111 and P112 in the DraB – yellow; P94 and P95 in the PapD - green).