Glycoside hydrolase subfamily GH5_57 features a highly redesigned catalytic interface to process complex hetero-β-mannans

Autor: Marcele P. Martins, Mariana A. B. Morais, Gabriela F. Persinoti, Rafael H. Galinari, Li Yu, Yoshihisa Yoshimi, Fernanda B. Passos Nunes, Tatiani B. Lima, Shayla F. Barbieri, Joana L. M. Silveira, Vincent Lombard, Nicolas Terrapon, Paul Dupree, Bernard Henrissat, Mário T. Murakami

Publikováno v: Martins, M P, Morais, M A B, Persinoti, G F, Galinari, R H, Yu, L, Yoshimi, Y, Passos Nunes, F B, Lima, T B, Barbieri, S F, Silveira, J L M, Lombard, V, Terrapon, N, Dupree, P, Henrissat, B & Murakami, M T 2022, ' Glycoside hydrolase subfamily GH5_57 features a highly redesigned catalytic interface to process complex hetero-β-mannans ', Acta Crystallographica Section D: Biological Crystallography, vol. 78, no. 11, pp. 1358-1372 . https://doi.org/10.1107/S2059798322009561
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2022, 78 (11), pp.1358-1372. ⟨10.1107/S2059798322009561⟩

International audience; Glycoside hydrolase family 5 (GH5) harbors diverse substrate specificities and modes of action, exhibiting notable molecular adaptations to cope with the stereochemical complexity imposed by glycosides and carbohydrates such a

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