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X-ray structure of the N-terminal domain of the flocculin Flo11 from Saccharomyces cerevisiaeX-ray structure of the N-terminal domain of the flocculin Flo11 from Saccharomyces cerevisiae
Structural highlights
FunctionFLO11_YEAST Cell wall protein that participates in adhesive cell-cell interactions during yeast flocculation, a reversible, asexual and Ca(2+)-dependent process in which cells adhere to form aggregates (flocs) consisting of thousands of cells. Also involved in cell-substrate adhesion, haploid invasive growth, diploid pseudohyphae formation and biofilm (flor) development. The precise mechanism by which this protein mediates adhesion is unclear but may involve homotypic binding. Adhesive activity is inhibited by mannose, but not by glucose, maltose, sucrose or galactose.[1] [2] [3] [4] [5] [6] [7] [8] [9] Publication Abstract from PubMedSaccharomyces cerevisiae harbors a family of GPI-anchored cell wall proteins for interaction with its environment. The flocculin Flo11, a major representative of these fungal adhesins, confers formation of different types of multicellular structures such as biofilms, flors, or filaments. To understand these environment-dependent growth phenotypes on a molecular level, we solved the crystal structure of the N-terminal Flo11A domain at 0.89-A resolution. Besides a hydrophobic apical region, the Flo11A domain consists of a beta sandwich of the fibronectin type III domain (FN3). We further show that homophilic Flo11-Flo11 interactions and heterophilic Flo11-plastic interactions solely depend on the Flo11A domain and are strongly pH dependent. These functions of Flo11A involve an apical region with its surface-exposed aromatic band, which is accompanied by acidic stretches. Together with electron microscopic reconstructions of yeast cell-cell contact sites, our data suggest that Flo11 acts as a spacer-like, pH-sensitive adhesin that resembles a membrane-tethered hydrophobin. Interactions by the Fungal Flo11 Adhesin Depend on a Fibronectin Type III-like Adhesin Domain Girdled by Aromatic Bands.,Kraushaar T, Bruckner S, Veelders M, Rhinow D, Schreiner F, Birke R, Pagenstecher A, Mosch HU, Essen LO Structure. 2015 Jun 2;23(6):1005-17. doi: 10.1016/j.str.2015.03.021. Epub 2015, May 7. PMID:25960408[10] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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