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Title: X-Ray Diffraction Structure of a plant Glycosyl Hydrolase family 32 protein: Fructan 1-Exohydrolase IIa of Cichorium intybus
Authors: Verhaest, Maureen ×
Van den Ende, Wim
Le Roy, Katrien
De Ranter, Camiel
Van Laere, André
Rabijns, Anja #
Issue Date: 2005
Publisher: Blackwell Science
Series Title: The Plant Journal vol:41 issue:3 pages:400-11
Abstract: Fructan 1-exohydrolase, an enzyme involved in fructan degradation, belongs to the glycosyl hydrolase family 32. The structure of isoenzyme 1-FEH IIa from Cichorium intybus is described at a resolution of 2.35 Å. The structure consists of an N-terminal fivefold β-propeller domain connected to two C-terminal β-sheets. The putative active site is located entirely in the β-propeller domain and is formed by amino acids which are highly conserved within glycosyl hydrolase family 32. The fructan-binding site is thought to be in the cleft formed between the two domains. The 1-FEH IIa structure is compared with the structures of two homologous but functionally different enzymes: a levansucrase from Bacillus subtilis (glycosyl hydrolase family 68) and an invertase from Thermotoga maritima (glycosyl hydrolase family 32).
ISSN: 0960-7412
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Administration Rectorial Services - miscellaneous
Faculty of Pharmaceutical Sciences - miscellaneous
Biocrystallography
Laboratory for Molecular Plant Physiology (-)
Molecular Physiology of Plants and Micro-organisms Section - miscellaneous
× corresponding author
# (joint) last author

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