Fig. 5
From: Structural basis for arginine glycosylation of host substrates by bacterial effector proteins
Binding modes of short peptide substrates. Binding epitope mappings of a FADD110-118 b TRADD229-237 and c, d GAPDH195-203 peptides in the presence of 25 μM SseK1. Samples in a, b and d contained 25 μM Mn2+, and 25 μM UDP. All STD intensities normalized against Hζ2 of the tryptophan. Colored circles represent magnitude of normalized intensities (blue:< 40%, pink: 40–70%, red:> 70%). Comparison of GAPDH195–203 binding to SseK1, c in the absence, and, d in the presence of Mn2+ and UDP, reveals a significant change in the binding mode of the substrate peptide upon addition of the cofactor and the nucleotide diphosphate. For STD NMR study of binding to SseK2 see Supplementary Fig. 5
