Structural and biochemical characterization of the N-terminal domain of flocculin Lg-Flo1p from Saccharomyces pastorianus reveals a unique specificity for phosphorylated mannose.

Unlabelled: The mechanism of yeast flocculation is generally considered to be mediated through the interaction of cell surface flocculins and mannan carbohydrates. In the present study, the crystal structure of the soluble 25-kDa lectin domain of flocculin 1 from brewer's yeast (Lg-Flo1p) was resolved to 2.5 Å, and its binding specificity towards oligosaccharides was investigated by fluorescence spectroscopy.

Purification, crystallization and preliminary X-ray diffraction analysis of the carbohydrate-binding domain of flocculin, a cell-adhesion molecule from Saccharomyces carlsbergensis.

The recombinant carbohydrate-binding domain of the cell-surface lectin flocculin from brewer's yeast has been identified, purified and crystallized. The expression of the protein is associated with the nutritional state of the yeast. P2(1)2(1)2(1) crystals with unit-cell parameters a = 36.