Title: X-ray diffraction structure of a cell-wall invertase from Arabidopsis thaliana
Authors: Verhaest, Maureen ×
Lammens, Willem
Le Roy, Katrien
De Coninck, Barbara
De Ranter, Camiel
Van Laere, André
Van den Ende, Wim
Rabijns, Anja #
Issue Date: Dec-2006
Series Title: Acta crystallographica. Section D, Biological crystallography vol:62 issue:Pt 12 pages:1555-1563
Abstract: Cell-wall invertases play crucial roles during plant development. They hydrolyse sucrose into its fructose and glucose subunits by cleavage of the alpha1-beta2 glycosidic bond. Here, the structure of the Arabidopsis thaliana cell-wall invertase 1 (AtcwINV1; gene accession code At3g13790) is described at a resolution of 2.15 A. The structure comprises an N-terminal fivefold beta-propeller domain followed by a C-terminal domain formed by two beta-sheets. The active site is positioned in the fivefold beta-propeller domain, containing the nucleophile Asp23 and the acid/base catalyst Glu203 of the double-displacement enzymatic reaction. The function of the C-terminal domain remains unknown. Unlike in other GH 32 family enzyme structures known to date, in AtcwINV1 the cleft formed between both domains is blocked by Asn299-linked carbohydrates. A preliminary site-directed mutagenesis experiment (Asn299Asp) removed the glycosyl chain but did not alter the activity profile of the enzyme.
ISSN: 1399-0047
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biocrystallography
Molecular Physiology of Plants and Micro-organisms Section - miscellaneous
Centre for Food and Microbial Technology
Administration Rectorial Services - miscellaneous
× corresponding author
# (joint) last author

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