Crystallization and preliminary X-ray diffraction analysis of the fructofuranosidase from Xanthophyllomyces dendrorhous.
Xanthophyllomyces dendrorhous invertase is an extracellular enzyme that releases β-fructose from the nonreducing termini of various β-D-fructofuranoside substrates. Its ability to produce neokestose by transglycosylation makes this enzyme an interesting research target for applications in industrial biotechnology. The native enzyme, which is highly glycosylated, failed to crystallize. Therefore, it was submitted to EndoH deglycosylating treatment and crystals were grown by vapour-diffusion methods. The crystals belonged to space group P2(1)2(1)2, with unit-cell parameters a = 75.29, b = 204.93, c = 146.25 Å. Several diffraction data sets were collected using a synchrotron source. Self-rotation function and gel-filtration experiments suggested that the enzyme is a dimer with twofold symmetry.
Departamento de Cristalografía y Biología Estructural, Instituto de Química-Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.
Aitana
A
Polo
Dolores
D
Linde
Marta
M
Estévez
María
M
Fernández-Lobato
Julia
J
Sanz-Aparicio
D001487:Basidiomycota / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D017510:Protein Folding; D055503:Protein Multimerization; D043324:beta-Fructofuranosidase / Q000737:chemistry* / Q000378:metabolism
D043324:beta-Fructofuranosidase