Journal Article

PUBDB-2025-04172

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Insights into a water-mediated catalytic triad architecture in CE20 carbohydrate esterases

Teune, M. ; Vieira, P. S. ; Döhler, T. ; Palm, G.Extern*EMBL* ; Dutschei, T. ; Bartosik, D. ; Berndt, L. ; Persinoti, G. F. ; Maaß, S. ; Becher, D. ; Schweder, T. ; Murakami, M. (Corresponding author)Extern* ; Lammers, M. (Corresponding author)Extern*EMBL* ; Bornscheuer, U. T. (Corresponding author)

2025
Springer Nature [London]

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Please use a persistent id in citations: doi:10.1038/s41467-025-62387-5  doi:10.3204/PUBDB-2025-04172

Abstract: Carbohydrate esterases modify polysaccharides by removing different ester moieties thereby affecting their physicochemical properties and their accessibility by glycoside hydrolases. We determined the full-length structures of two members (Fl8CE20_II and PpCE20_II) from the carbohydrate esterase family 20 (CE20) by X-ray crystallography that feature an ancillary domain, inserted into the catalytic SGNH-hydrolase domain. Detailed structural analysis identifies a so far undescribed catalytic triad architecture which lacks the typical aspartate for polarization of the histidine but instead reveals a precisely coordinated water molecule mediating contact between the His and Asp. This coordinated water in the Ser-His-(H2O-Asp/Asn) motif, as further confirmed by mutational studies and by determination of kinetic constants, is crucial for catalytic activity. We therefore term this active site architecture a water-mediated catalytic triad.

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Contributing Institute(s):

1. EMBL-User (EMBL-User)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)
2. DFG project G:(GEPRIS)277249973 - FOR 2406: Proteogenomik der Marinen Polysaccharid Verwertung (POMPU) (277249973) (277249973)

Experiment(s):

1. PETRA Beamline P13 (PETRA III)

Appears in the scientific report 2025

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