Structures of α-galactosaminidases from the CAZy GH114 family and homologs defining a new GH191 family of glycosidases

Roth, C.; Moroz, O.V.; Miranda, S.A.D.; Jahn, L.; Blagova, E.V.; Lebedev, A.A.; Segura, D.R.; Stringer, M.A.; Friis, E.P.; Franco Cairo, J.P.L.; Davies, G.J.; Wilson, K.S.

doi:10.1107/S2059798325002864

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

IUCr IT WDC

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Figure 4
Structure of a bacterial GH191 enzyme. (a) Ribbon representation of TmGH191 in light brown. (b) Ribbon representation of TmGH191 coloured from the N-terminus to the C-terminus in blue to red, with the van der Waals surface in grey showing the substrate crevice in the middle of the protein on the C-terminal side of the barrel. (c) Overlay of TmGH191 in light brown with Env-GH191 in dark brown. (d) Overlay of TmGH191 in light brown with Env-GH191 in dark brown, FsGH114 in dark blue, AfGH114 (Ega3; PDB entry 6oj1) in light blue, AcSph3 (PDB entry 5c5g) in gold and PaPelA_H (PDB entry 5tcb) in lilac. (e) Close-up of the two active-site residues in the GH191 family and GH114 enzymes with the aspartate as the nucleophile and the glutamate as a general acid/base. The residue numbering is for TmGH191, Env-GH191, AfGH114, FsGH114, AcSph3 and PaPelA_H, respectively. This figure, as well as Figs. 5