Figure 3: The catalytic mechanism of GtrB. | Nature Communications

Figure 3: The catalytic mechanism of GtrB.

From: Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis

Figure 3

(a) The disposition of key residues in the active site and interactions with the acceptor and donor substrates. An anomalous difference Fourier map (contoured at 5 σ above the mean) calculated from a tungstate-soaked wild-type (WT) crystal is represented as purple mesh. Residues D94, D96, R122, D157, R200 and the UDP are shown in stick representation. Mn2+ is represented as a purple sphere. (b) Mutation of key residues in the acceptor and donor sites abolishes GtrB activity. (c) The catalytic mechanism of GtrB does not require a catalytic base. Error bars are provided as s.e.m., n=3.

Back to article page