Structural and functional significance of two conserved lysine residues in acylated sites of Kingella kingae RtxA cytotoxin

Data underlying the figures in the publication “Structural and functional significance of two conserved lysine residues in acylated sites of Kingella kingae RtxA cytotoxin”, published in Biochimie, 2024 Dec 31:S0300-9084(24)00320-1. https://doi.org/10.1016/j.biochi.2024.12.016 Description of Files: THS_2A: Functional complementation of four different fusion pairs, quantified by measuring β-galactosidase activity in bacterial extracts of E. coli strain BTH101. THS_2B: Functional complementation of T25-RtxC with T18-proRtxA529–718 fusion variants. THS_2C: Functional complementation of T25-RtxC with T18-proRtxA529–623, T18-proRtxA624–718, or T18-proRtxA529–718. THS_2D: Functional complementation of T25-RtxC with T18-proRtxA529–623 fusion variants containing substitutions K558R and K558Q. THS_2E: Functional complementation of T25-RtxC with the T18-proRtxA624–718 fusion variants containing substitutions K689R and K689Q. Binding_3BL: Cell binding of RtxA variants to sheep erythrocytes. Binding_3BR: Cell binding of RtxA variants to sheep erythrocytes after washing with alkaline carbonate. Far-UV_3CL: Far-UV spectra of RtxA variants. Near-UV_3CR: Near-UV spectra of RtxA variants. Lysis_4A: Erythrocyte lysis in the presence of RtxA variants.