Data sets on the interaction of FKBP35 from Plasmodium knowlesi and Hsp90 C-terminal pentapeptide

FK506-binding protein 35 from Plasmodium knowlesi (Pk-FKBP35) is a multidomain peptidyl-prolyl cis-trans isomerase (PPIase) considered a potential target for antimalarial drug development. The protein consists of an N-terminal FK506-binding domain (FKBD) and a tetratricopeptide repeat domain (TPRD) containing a calmodulin-binding motif (CBM). The TPRD domain is known to recognize the conserved MEEVD motif located at the C-terminus of heat shock protein 90 (Hsp90). This dataset describes the biochemical and biophysical characterization of Pk-FKBP35 and its interaction with the Hsp90-derived MEEVD motif. Recombinant full-length FKBP35 (FL-FKBP35) and three variants, namely Pk-FKBD, Pk-TPRD+, and a calmodulin-binding motif deletion mutant (del-CBM), were heterologously expressed in E. coli and purified to high purity. Circular dichroism spectroscopy confirmed the structural integrity of the recombinant proteins. PPIase activity assays using a fluorogenic substrate demonstrated that FL-FKBP35, Pk-FKBD, and del-CBM exhibited catalytic activity, with kcat/K_M values of 5.04 ± 0.21 × 10^-5, 4.81 ± 0.34 × 10^-5, and 5.17 ± 0.17 × 10^-5 M^-1 s^-1, respectively, whereas Pk-TPRD+ showed no detectable activity. Interactions between FKBP35 proteins and the MEEVD peptide were examined using surface plasmon resonance analysis, revealing that the dissociation constant (KD) of FL-FKBP35 (54.75 ± 5.01 µM) was comparable (P > 0.05) to that of Pk-TPRD+ (46.41 ± 5.36 µM), while Pk-FKBD alone showed no detectable binding. Functional assays further demonstrated that MEEVD binding did not significantly affect the intrinsic PPIase activity of FKBP35 (P > 0.05). These data provide detailed biochemical, biophysical, and interaction profiles of Pk-FKBP35 and its interaction with the Hsp90-derived MEEVD motif.