Fig. 1: Identification of the enzyme catalyzing LD1,3-crosslink. | Nature Communications

Fig. 1: Identification of the enzyme catalyzing LD1,3-crosslink.

From: A distinctive family of L,D-transpeptidases catalyzing L-Ala-mDAP crosslinks in Alpha- and Betaproteobacteria

Fig. 1

A Representative UV chromatogram of Gluconobacter oxydans peptidoglycan profile in stationary phase. LD1,3-crosslinked muropeptides are indicated in green. Underneath, heatmap representing the relative abundance of each muropeptide in representative bacteria species from the Acetobacteraceae family (Acetobacter pasteurianus and G. oxydans) and model organisms Escherichia coli and Vibrio cholerae. Schematic structures and nomenclature of the main muropeptides and crosslink type are shown. B Scheme of the in silico search of YkuD-domain containing enzyme candidates responsible for LD1,3-crosslinking. C Representative UV chromatograms of G. oxydans (Go) wild-type (WT), Δgox1074 and Δgox1074 pGox1074 complemented strains. LD1,3-crosslinked muropeptides are highlighted in green. D Domain analysis of Gox1074. Details of the LDT conserved motif in the YkuD domain including the catalytic Cys and His residues highlighted in yellow.

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