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Title: An alternate sucrose binding mode in the E203Q Arabidopsis invertase mutant: An X-ray crystallography and docking study
Authors: Matrai, Janka *
Lammens, Willem *
Jonckheer, Abel
Le Roy, Katrien
Rabijns, Anja
Van den Ende, Wim
De Maeyer, Marc # ×
Issue Date: 2008
Publisher: John Wiley & Sons
Series Title: Proteins: structure, function and genetics vol:71 issue:2 pages:552-564
Abstract: In the present study, we report on the X-ray crystallographic structure of a GH32 invertase mutant, (i.e., the Arabidopsis thaliana cell-wall invertase 1-E203Q, AtcwINV1-mutant) in complex with sucrose. This structure was solved to reveal the features of sugar binding in the catalytic pocket. However, as demonstrated by the X-ray structure the sugar binding and the catalytic pocket arrangement is significantly altered as compared with what was expected based on previous X-ray structures on GH-J clan enzymes. We performed a series of docking and molecular dynamics simulations on various derivatives of AtcwINV1 to reveal the reasons behind this modified sugar binding. Our results demonstrate that the E203Q mutation introduced into the catalytic pocket triggers conformational changes that alter the wild type substrate binding. In addition, this study also reveals the putative productive sucrose binding modus in the wild type enzyme. Proteins 2008. (c) 2007 Wiley-Liss, Inc.
URI: 
ISSN: 0887-3585
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biochemistry, Molecular and Structural Biology Section
Vesalius Research Centre (-)
Molecular Physiology of Plants and Micro-organisms Section - miscellaneous
Centre for Food and Microbial Technology
Faculty of Pharmaceutical Sciences - miscellaneous
Biocrystallography
Research Group Neurophysiology
Laboratory for Auditive Neurophysiology
* (joint) first author
× corresponding author
# (joint) last author

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