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Fig. 5 | BMC Genomics

Fig. 5

From: Bioinformatics comparisons of RNA-binding proteins of pathogenic and non-pathogenic Escherichia coli strains reveal novel virulence factors

Fig. 5

Modelling of the RNase PH proteins from two different E. coli strains. The structural modelling of the RNase PH protein has been represented in this figure. a Schematic diagram of the active (above) and the inactive (below) RNase PH proteins. The RNase PH and the RNase_PH_C domains, as defined by Pfam (v.28), have been represented in magenta and pink, respectively. The five residues that have undergone mutations due to a point deletion and the ten residues that are missing from the inactive RNase PH protein from strain K12 have been depicted in orange and yellow, respectively. These two sets of residues are the ones of interest in this study. b Model of the RNase PH monomer from strain O26:H11. The residues with the same colour codes as mentioned in panel (a), have been represented on the structure of the model. The residues that are within an 8 Å cut-off distance from the residues of interest have been highlighted in cyan (left). c Structure of the RNase PH hexamer from strain O26:H11 (left) and the probable structure of the inactive RNase PH hexamer from strain K12 (right). The dimers marked in black boxes are the ones that were randomly selected for MD simulations. d Electrostatic potential on the solvent accessible surface of the RNase PH hexamer from strain O26:H11 (left) and that of the inactive RNase PH hexamer from strain K12 (right)

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