2NBH

Solution structure of the HYD1 hydrophobin from Schizophyllum commune

2NBH の概要

• エントリーDOI: 10.2210/pdb2nbh/pdb
• NMR情報: BMRB: 25976
• 分子名称: Fungal hydrophobin (1 entity in total)
• 機能のキーワード: protein fibril
• 由来する生物種: Schizophyllum commune H4-8 (Split gill fungus)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10873.47

構造登録者

Langelaan, D.,Smith, S.,Grondin, J. (登録日: 2016-02-21, 公開日: 2016-03-16, 最終更新日: 2024-11-27)

主引用文献

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

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: 28393921
DOI: 10.1038/srep45863

実験手法

SOLUTION NMR