4gq7

Crystal structure of Lg-Flo1p

spinqualitylabelsall models 4gq7, resolution 2.53Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4gq7 is a 1 chain structure with sequence from Saccharomyces pastorianus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.53Å Ligands: CA, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B3IUA8_SACPS 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Flocculation protein 3D structures

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