Fig. 5: Targeting peptide mutational analysis. | Nature Communications

Fig. 5: Targeting peptide mutational analysis.

From: Structural basis for peroxidase encapsulation inside the encapsulin from the Gram-negative pathogen Klebsiella pneumoniae

Fig. 5

a TP sequence highlighting all residues subjected to mutational analysis (underlined) colored by the specific characteristics defined below. b Overview of all TP and KpEnc protomer mutants created. Residues are colored as in (a) (yellow, hydrophobic; blue, cationic; green, flexible; red, hydrogen bonding). TP residues with resolved cryo-EM density are highlighted in the wild-type sequence (WT; black outline). KpEnc protomer mutants (Enc) shown at the bottom. c KpEnc protomer viewed from the shell interior highlighting TP-binding site mutations. The TP is shown as semi-transparent yellow surface. d Representative SDS-PAGE gels of purified cargo-loaded encapsulins for the WT and respective mutants showing KpEnc (upper band) and the co-purified encapsulated SUMO-TP mutant cargo (lower band). Source data are provided as a Source Data file. e Loading percentages of all SUMO-TP mutants as determined by gel densitometry. Loading percentage was normalized to WT loading. Data are shown as mean values. Error bars represent standard deviation of three independent experiments. Numbering and coloring are the same as in the preceding panels. Source data are provided as a Source Data file.

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