4UYR

X-ray structure of the N-terminal domain of the flocculin Flo11 from Saccharomyces cerevisiae

Summary for 4UYR

• Entry DOI: 10.2210/pdb4uyr/pdb
• Related: 4UYS 4UYT
• Descriptor: FLOCCULATION PROTEIN FLO11, SODIUM ION, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: cell adhesion, saccharomyces cerevisiae, flo11, adhesin, flocculation, hydrophobic patches, homotypic binding
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Secreted, cell wall: P08640
• Total number of polymer chains: 1
• Total formula weight: 23914.21

Authors

Veelders, M.,Kraushaar, T.,Brueckner, S.,Rhinow, D.,Moesch, H.U.,Essen, L.O. (deposition date: 2014-09-03, release date: 2015-08-12, Last modification date: 2024-10-23)

Primary citation

Kraushaar, T.,Bruckner, S.,Veelders, M.,Rhinow, D.,Schreiner, F.,Birke, R.,Pagenstecher, A.,Mosch, H.,Essen, L.
Interactions by the Fungal Flo11 Adhesin Depend on a Fibronectin Type III-Like Adhesin Domain Girdled by Aromatic Bands.
Structure, 23:1005-, 2015

PubMed Abstract: Saccharomyces 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-Å resolution. Besides a hydrophobic apical region, the Flo11A domain consists of a β 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.

PubMed: 25960408
DOI: 10.1016/J.STR.2015.03.021

Experimental method

X-RAY DIFFRACTION (0.89 Å)