Extended Data Fig. 3: Comparison of MccB/subtiligase-catalysed and eSrtA-catalysed C-terminal protein modification. | Nature Chemistry

Extended Data Fig. 3: Comparison of MccB/subtiligase-catalysed and eSrtA-catalysed C-terminal protein modification.

From: Engineered reactivity of a bacterial E1-like enzyme enables ATP-driven modification of protein and peptide C termini

Extended Data Fig. 3

(a) MccB/subtiligase-catalysed C-terminal peptide ligation to GS-GFP-TeCH. In the absence of peptide nucleophile, MccB and subtiligase catalyse GS-GFP cyclization, but this reaction is efficiently suppressed in the presence of 5 mM Ala-Phe. (b) eSrtA-catalysed C-terminal modification of GS-GFP-LPETGG. In the absence of nucleophile, eSrtA catalyzes GFP cyclization that cannot be completely suppressed even in the presence of 10 mM GGG peptide. (c) eSrtA cyclization is suppressed by removing the N-terminal GS sequence at the N terminus of GS-GFP-LPETGG.

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