Structure–function characterization of cellulose synthase: relationship to other glycosyltransferases

摘要: Abstract A combined structural and functional model of the catalytic region cellulose synthase is presented as a prototype for action processive β-glycosyltransferases other glycosyltransferases. 285 amino acid segment Acetobacter xylinum containing all conserved residues in globular was subjected to protein modeling using genetic algorithm. This folds into single large domain with topology exhibiting mixed alpha/beta structure. The predicted structure serves topological outline this β-glycosyltransferase. By incorporating new site-directed mutagenesis data comparative analysis aspartic QXXRW motif we deduce number implications based on includes location UDP–glucose substrate-binding cavity, suggestions processing including positions residues, secondary arrangement organization. Comparisons synthases from higher plants (genetic algorithm cotton CelA1), neural network predictions (PHD), recently experimentally determined structures non-processive SpsA β4-galactosyltransferase retest further validate our structure-function description glycosyltransferase.