4gq7

Publication Abstract from PubMed

The mechanism of yeast flocculation is generally accepted to be mediated through interaction of cell surface flocculins and mannan carbohydrates. Here, the crystal structure of the soluble 25 kDa lectin domain of Lg-Flo1p flocculin from brewer's yeast was solved to 2.5 A, and its binding specificity towards oligosaccharides investigated by fluorescence spectroscopy. Lg-Flo1p displays broad specificity towards sugars, and interestingly has a 14-fold higher affinity for mannose-1-phosphate and glucose-1-phosphate, compared to their unphosphorylated counterparts. Through structural analysis, we propose that this higher affinity is due to charge interaction with a lysine residue in a carbohydrate binding loop region, NAKAL, unique to NewFlo type flocculins. This raises the possibility of a unique mechanism of flocculation in NewFlo type yeast, which recognizes phosphorylated cell-surface mannans. (c) 2013 Carlsberg Laboratory. Journal compilation (c) 2013 FEBS.

Structural and biochemical characterization of the N-terminal domain of flocculin, Lg-Flo1p from Saccharomyces pastorianus reveal a unique specificity for phosphorylated mannose.,Sim L, Groes M, Olesen K, Henriksen A FEBS J. 2013 Jan 2. doi: 10.1111/febs.12102. PMID:23281814^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.