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![[Figure 4]](rr5249fig4mag.jpg)
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Figure 4
Catalytic mechanism and structure of 6-acetamido-6-deoxy-castanospermine. (a) Neighbouring-group participation catalytic mechanism of DspB. Here, we show the intermediate as a charged oxazolinium ion as predicted from calculations on related systems (Calvelo et al., 2023  ). (b) Structure of 6-Ac-Cas. (c) Dispersin inhibition by 6-Ac-Cas. Thermodynamics of binding: the raw data are shown in the baseline-adjusted injection profile (top) and the titration curve with one-site fitting in red (bottom). Left: DispTs2, 0.93 ± 0.004 sites, −36.7 ± 0.2 kJ mol−1. Middle: DispLp, 0.90 ± 1.36 sites, −19.1 ± 0.35 kJ mol−1. Right: DispSf, 1.1 ± 0.02 sites, 26.4 ± 1.11 kJ mol−1. (d) Active-site residues of DispLp and water molecules with 6-Ac-Cas in complex. Hydrogen bonds are represented by dashed black lines and the maximum-likelihood/σA-weighted 2Fobs − Fcalc map is shown in green contoured at 0.90 e Å−3. (e) Scheme of DispLp active-site residue interactions with 6-Ac-Cas. |
![[Figure 4]](rr5249fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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