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- W2605401528 abstract "Abstract Class I hydrophobins are functional amyloids secreted by fungi. They self-assemble into organized films at interfaces producing structures that include cellular adhesion points and hydrophobic coatings. Here, we present the first structure and solution properties of a unique Class I protein sequence of Basidiomycota origin: the Schizophyllum commune hydrophobin SC16 ( hyd1 ). While the core β-barrel structure and disulphide bridging characteristic of the hydrophobin family are conserved, its surface properties and secondary structure elements are reminiscent of both Class I and II hydrophobins. Sequence analyses of hydrophobins from 215 fungal species suggest this structure is largely applicable to a high-identity Basidiomycota Class I subdivision (IB). To validate this prediction, structural analysis of a comparatively distinct Class IB sequence from a different fungal order, namely the Phanerochaete carnosa PcaHyd1, indicates secondary structure properties similar to that of SC16. Together, these results form an experimental basis for a high-identity Class I subdivision and contribute to our understanding of functional amyloid formation." @default.
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- W2605401528 date "2017-04-10" @default.
- W2605401528 modified "2023-10-06" @default.
- W2605401528 title "Characterization of a Basidiomycota hydrophobin reveals the structural basis for a high-similarity Class I subdivision" @default.
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- W2605401528 doi "https://doi.org/10.1038/srep45863" @default.
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