4GQ7

Crystal structure of Lg-Flo1p

4GQ7 の概要

• エントリーDOI: 10.2210/pdb4gq7/pdb
• 分子名称: Flocculin, CALCIUM ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: carbohydrate binding domain, pa14 domain, sugar binding protein
• 由来する生物種: Saccharomyces pastorianus (Saccharomyces carlsbergensis)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25152.68

構造登録者

Sim, L.,Groes, M.,Olesen, K.,Henriksen, A. (登録日: 2012-08-22, 公開日: 2013-01-16, 最終更新日: 2023-09-13)

主引用文献

Sim, L.,Groes, M.,Olesen, K.,Henriksen, A.
Structural and biochemical characterization of the N-terminal domain of flocculin Lg-Flo1p from Saccharomyces pastorianus reveals a unique specificity for phosphorylated mannose.
Febs J., 280:1073-1083, 2013

PubMed Abstract: 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. Lg-Flo1p displays broad specificity towards sugars and has a 14-fold higher affinity for mannose 1-phosphate and glucose 1-phosphate compared to their unphosphorylated counterparts. Based on the results of a structural analysis, we propose that this higher affinity is the result of a 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.

PubMed: 23281814
DOI: 10.1111/febs.12102

実験手法

X-RAY DIFFRACTION (2.53 Å)