2nbh
Solution structure of the HYD1 hydrophobin from Schizophyllum communeSolution structure of the HYD1 hydrophobin from Schizophyllum commune
Structural highlights
Publication Abstract from PubMedClass 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 beta-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. Characterization of a Basidiomycota hydrophobin reveals the structural basis for a high-similarity Class I subdivision.,Gandier JA, Langelaan DN, Won A, O'Donnell K, Grondin JL, Spencer HL, Wong P, Tillier E, Yip C, Smith SP, Master ER Sci Rep. 2017 Apr 10;7:45863. doi: 10.1038/srep45863. PMID:28393921[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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