Extended Data Fig. 5: Active site of SN243 variants co-crystallized with reaction substrates and product.
From: Functional metagenomic screening identifies an unexpected β-glucuronidase
The structures of SN243 wt co-crystallized with GlcA (PDB: 7QE2) (a) and of the inactive mutant SN243D415A with FD-β-GlcA (PDB: 7QEA) (b) and pNP-β-GlcA (PDB: 7QEF) (c) bound in the active site were obtained at 2.15 Å, 2.28 Å and 2.41 Å, respectively. The gray mesh shows the Fo-Fc map for GlcA (a), FD-β-GlcA (b) and pNP-β-GlcA (c) contoured at 2 σ. As no electron density was observed for the second GlcA moiety of the FD-β-GlcA ligand in (b), the monoglycosylated substrate was modeled.
