2NBH
Solution structure of the HYD1 hydrophobin from Schizophyllum commune
Summary for 2NBH
| Entry DOI | 10.2210/pdb2nbh/pdb |
| NMR Information | BMRB: 25976 |
| Descriptor | Fungal hydrophobin (1 entity in total) |
| Functional Keywords | protein fibril |
| Biological source | Schizophyllum commune H4-8 (Split gill fungus) |
| Total number of polymer chains | 1 |
| Total formula weight | 10873.47 |
| Authors | Langelaan, D.,Smith, S.,Grondin, J. (deposition date: 2016-02-21, release date: 2016-03-16, Last modification date: 2024-11-27) |
| Primary citation | Gandier, J.A.,Langelaan, D.N.,Won, A.,O'Donnell, K.,Grondin, J.L.,Spencer, H.L.,Wong, P.,Tillier, E.,Yip, C.,Smith, S.P.,Master, E.R. Characterization of a Basidiomycota hydrophobin reveals the structural basis for a high-similarity Class I subdivision. Sci Rep, 7:45863-45863, 2017 Cited by PubMed 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. PubMed: 28393921DOI: 10.1038/srep45863 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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