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. Author manuscript; available in PMC: 2018 Jul 25.
Published in final edited form as: Nature. 2018 Jan 17;553(7689):496–500. doi: 10.1038/nature25442

Extended Data Figure 1. Schematic representation of the SrtA reaction.

Extended Data Figure 1

SrtA enzyme recognizes the short amino acid sequence LPXTG (where X is any amino acid). Upon binding, SrtA forms a covalent acyl intermediate between the threonine of the substrate and the cysteine present in its catalytic pocket. The reaction proceeds with the formation of an amide bond between substrate threonine and an N-terminal glycine. Affinities displayed refer to engineered SrtA variants carrying mutations P94S, D160N, and K196T.