Title: Crystal structures of Arabidopsis thaliana cell-wall invertase mutants in complex with sucrose
Authors: Lammens, Willem
Le Roy, Katrien
Van Laere, André
Rabijns, Anja
Van den Ende, Wim # ×
Issue Date: Mar-2008
Publisher: Academic press ltd elsevier science ltd
Series Title: Journal of Molecular Biology vol:377 issue:2 pages:378-385
Abstract: In plants, cell-wall invertases fulfil important roles in carbohydrate partitioning, growth, development and crop yield. In this study, we report on different X-ray crystal structures of Arabidopsis thaliana cell-wall invertase 1 (AtcwINV1) mutants with sucrose. These structures reveal a detailed view of sucrose binding in the active site of the wild-type AtcwINV1. Compared to related enzyme-sucrose complexes, important differences in the orientation of the glucose subunit could be observed. The structure of the E203Q AtcwINV1 mutant showed a complete new binding modus, whereas the D23A, E203A and D239A structures most likely represent the productive binding modus. Together with a hydrophobic zone formed by the conserved W20, W47 and W82, the residues N22, D23, R148, E203, D149 and D239 are necessary to create the ideal sucrose-binding pocket. D239 can interact directly with the glucose moiety of sucrose, whereas K242 has an indirect role in substrate stabilization. Most probably, K242 keeps D239 in a favourable position upon substrate binding. Unravelling the exact position of sucrose in plant cell-wall invertases is a necessary step towards the rational design of superior invertases to further increase crop yield and biomass production. (C) 2007 Elsevier Ltd. All rights reserved.
ISSN: 0022-2836
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular Physiology of Plants and Micro-organisms Section - miscellaneous
Centre for Food and Microbial Technology
Faculty of Pharmaceutical Sciences - miscellaneous
× corresponding author
# (joint) last author

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