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Receveur-Brechot, V ; Czjzek, M ; Barre, A ; Roussel, A ; Peumans, WJ ; Van Damme, EJM ; Rouge, P
Crystal structure at 1.45-A resolution of the major allergen endo-ß-1,3-glucanase of banana as a molecular basis for the latex-fruit syndrome
Proteins-Structure Function and Bioinformatics 63 (1) 235-242
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Abstract :
Resolution of the crystal structure of the banana fruit endo-ß-1,3-glucanase by synchrotron X-ray diffraction at 1.45-angstrom resolution revealed that the enzyme possesses the eightfold ß/a architecture typical for family 17 glycoside hydrolases. The electronegatively charged catalytic central cleft harbors the two glutamate residues (Glu94 and Glu236) acting as hydrogen donor and nucleophile residue, respectively. Modeling using a ß-1,3 linked glucan trisaccharide as a substrate confirmed that the enzyme readily accommodates a ß-1,3-glycosidic linkage in the slightly curved catalytic groove between the glucose units in positions -2 and -1 because of the particular orientation of residue Tyr33 delimiting subsite-2.