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. 2023 Mar 1;14:1170. doi: 10.1038/s41467-023-36280-y

Fig. 3. Crystal structure of the CpoBD13:PA complex.

Fig. 3

a Three-dimensional structure of CpoBD13 determined by X-ray crystallography superimposed with HBD-2 (PDB ID 1FD3). Zoomed in region shows the substitution of K36 (a crucial residue for membranolytic activity) in HBD-2 for H35 in CpoBD13. b Four CpoBD13 chains are found in the asymmetric unit (white, cyan, steel blue and magenta cartoon), bound to four PA molecules shown as green sticks. c Type I and d Type II PA binding sites. Key interacting residues are shown as sticks. Hydrogen bonds or ionic interactions are marked as black dashed lines. Schematic representation of the e Type I and f Type II PA binding sites. g CpoBD13:PA complex forms a single-stranded left-handed helix. The coil shown comprises the content of four asymmetric units. The location of a single type I PA binding site is boxed in black.