Fig. 3 | Nature Communications

Fig. 3

From: Structural basis for arginine glycosylation of host substrates by bacterial effector proteins

Fig. 3

UDP-GlcNAc binding mode in SseK2. a Uracil moiety of UDP-GlcNAc interacts with SseK2 through hydrogen bonds and π-π stacking (top panel), but SseK1 uses a slightly different mechanism (second and third panel). Uracil binding mode of SseK3 is similar to SseK2 instead of SseK1 (bottom panel). b GlcNAc moiety of UDP-GlcNAc interacts with Asp204, Arg207, Asp239, and Arg348 by hydrogen bonds. The carbonyl group of the acetyl of GlcNAc interacts with a water molecule to stabilize the divalent metal ion. c Manganese ion coordinates six oxygens from pyrophosphate, Ser340, Asn338, Asp241, and water. The DxD motif stabilizes both UDP-GlcNAc and manganese ion. *Amino acid numbering in brackets refers to conserved sequence of SseK1. Black dashed lines represent hydrogen bonds

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