Expansion of the diversity of dispersin scaffolds

Males, A.; Moroz, O.V.; Blagova, E.; Munch, A.; Hansen, G.H.; Johansen, A.H.; Østergaard, L.H.; Segura, D.R.; Eddenden, A.; Due, A.V.; Gudmand, M.; Salomon, J.; Sørensen, S.R.; Franco Cairo, J.P.L.; Nitz, M.; Pache, R.A.; Vejborg, R.M.; Bhosale, S.; Vocadlo, D.J.; Davies, G.J.; Wilson, K.S.

doi:10.1107/S205979832500110X

Acta Crystallographica Section D
Acta Crystallographica
Section DSTRUCTURAL BIOLOGY

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Figure 7
Conserved residues in GH20 enzymes are clustered in the active site and on the top face. (a) Surface representation of DspB (PDB entry 1yht) in white with residues coloured according to the degree of sequence conservation using the aligned proteins from Fig. 1

. GlcNAc, in yellow, was modelled into the active site by superimposing DspB (PDB entry 1yht) with a β-N-acetylhexosaminidase from Akkermansia muciniphila (PBD entry 7cbo; Xu et al., 2020

). This figure was produced using the ConSurf server (Landau et al., 2005

; Ashkenazy et al., 2016

). (b) Ribbon representation of DspB (PDB entry 1yht) with conserved residues specific to the dispersin subfamily members (not conserved in other GH20 enzymes) highlighted in yellow. (c) A close-up view of the dispersin active site in the example of DispB (PDB entry 1yht), with key residues numbered for DspB. NAG-thiazoline (NGT) from the DispTs2–di-NAG-thiazoline complex structure (PDB entry 9hta), in semi-transparent grey, is shown to indicate the ligand-binding site.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 81| Part 3| March 2025| Pages 130-146

https://doi.org/10.1107/S205979832500110X

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