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2XJP

X-ray structure of the N-terminal domain of the flocculin Flo5 from Saccharomyces cerevisiae in complex with calcium and mannose

Summary for 2XJP
Entry DOI10.2210/pdb2xjp/pdb
Related2XJQ 2XJR 2XJS 2XJT 2XJU 2XJV
DescriptorFLOCCULATION PROTEIN FLO5, CALCIUM ION, SODIUM ION, ... (7 entities in total)
Functional Keywordscell adhesion, greenbeard, pa14-domain, carbohydrate binding, social interaction
Biological sourceSACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
Total number of polymer chains1
Total formula weight28434.57
Authors
Veelders, M.,Brueckner, S.,Ott, D.,Unverzagt, C.,Moesch, H.-U.,Essen, L.-O. (deposition date: 2010-07-06, release date: 2010-12-15, Last modification date: 2024-10-16)
Primary citationVeelders, M.,Brueckner, S.,Ott, D.,Unverzagt, C.,Moesch, H.-U.,Essen, L.-O.
Structural Basis of Flocculin-Mediated Social Behavior in Yeast
Proc.Natl.Acad.Sci.USA, 107:22511-, 2010
Cited by
PubMed Abstract: In the budding yeast Saccharomyces cerevisiae, self-recognition and the thereby promoted aggregation of thousands of cells into protective flocs is mediated by a family of cell-surface adhesins, the flocculins (Flo). Based on this social behavior FLO genes fulfill the definition of "greenbeard" genes, which direct cooperation toward other carriers of the same gene. The process of flocculation plays an eminent role in the food industry for the production of beer and wine. However, the precise mode of flocculin-mediated surface recognition and the exact structure of cognate ligands have remained elusive. Here, we present structures of the adhesion domain of a flocculin complexed to its cognate ligands derived from yeast high-mannose oligosaccharides at resolutions up to 0.95 Å. Besides a PA14-like architecture, the Flo5A domain reveals a previously undescribed lectin fold that utilizes a unique DcisD calcium-binding motif for carbohydrate binding and that is widely spread among pro- and eukaryotes. Given the high abundance of high-mannose oligosaccharides in yeast cell walls, the Flo5A structure suggests a model for recognition, where social non-self- instead of unsocial self-interactions are favored.
PubMed: 21149680
DOI: 10.1073/PNAS.1013210108
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (0.95 Å)
Structure validation

229380

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