Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. family GH3 β-d-glucosidases

Agirre, J.; Ariza, A.; Offen, W.A.; Turkenburg, J.P.; Roberts, S.M.; McNicholas, S.; Harris, P.V.; McBrayer, B.; Dohnalek, J.; Cowtan, K.D.; Davies, G.J.; Wilson, K.S.

doi:10.1107/S2059798315024237

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 4
Three-dimensional fold, domain organization and asymmetric unit packing of AfβG and AoβG. Both enzymes have three domains (A, yellow; B, pink; C, light blue), with a dimer being the preferred biological arrangement. AoβG has two dimers in the asymmetric unit, with all of the sugars facing opposite sides. The sugars are shown as glycoblocks, with blue squares for N-acetyl-β-D-glucosamine and green circles for D-mannopyranose.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 72| Part 2| January 2016| Pages 254-265

doi:10.1107/S2059798315024237

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