Extended Data Fig. 4: Kinetic and structural analysis of BuS1_11.
From: Metabolism of a hybrid algal galactan by members of the human gut microbiome
a, kinetic analysis of neoporphyrabiose hydrolysis by BpS1_11*. The data is shown as the mean ± standard deviation of n = 3 independent reactions (see Supplementary Fig. 2 for independent data points). The solid line shows the best fit line to the Michaelis-Menton equation. b, the overall fold of BpS1_11 shown as a cartoon. The bound calcium ion is shown as a green sphere and key residues in the active site are shown as blue sticks. c, electron density maps of NP2 (yellow sticks) bound to the BuS1_11 active site are shown with the 2Fo-Fc map at 1σ in blue (top) and the Fo-Fc omit map at 3σ in green (bottom). d, the solvent accessible surface of the active site is shown in transparent grey with the bound NP2 as yellow sticks. The subsites of the active site are labeled in red according to the nomenclature of Hettle et al.27. e, structural overlap of BuS1_11 (blue) with BT4656 (grey, 5G2V). NP2 is shown as yellow sticks and 2-N,6-O-disulfo-d-glucosamine bound to BT4656 shown as green sticks. Relevant inserted structural motifs in each protein that contribute to carbohydrate specificity are shown as solid cartoons.
