Fig. 7: Third binding site of Api88 within domain III of the large ribosomal subunit. | Nature Communications

Fig. 7: Third binding site of Api88 within domain III of the large ribosomal subunit.

From: Multimodal binding and inhibition of bacterial ribosomes by the antimicrobial peptides Api137 and Api88

Fig. 7

a Cryo-EM density map of 50S•Api88 and the location of the three identified Api88 binding sites (orange) on the 50S subunit (blue). b Cross section along the Api88 tunnel, tunnel end and third binding site. c Cryo-EM density map of Api88 (orange) in binding site 3 and corresponding atomic model. d–e Molecular interactions of Api88 with surrounding rRNA residues. Hydrogen bonds are shown as dashed lines. f Calculated surface model of Api88 in its third binding site, sandwiched by rRNA helices H49 and H51 at 4 Å resolution. g Electrostatic surface potentials of the respective region. Coulombic electrostatic potentials are shown in red (electronegative; −10 kcal/mol·e), white (neutral; 0 kcal/mol·e) and blue (electropositive; 10 kcal/mol·e). h Rotated view of g from below H51. For clarity, Api88 is highlighted using a transparent sphere model in electrostatic representations.

Back to article page