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首页> 外文期刊>Journal of Molecular Biology >Analysis of the structure and conformational states of DewA gives insight into the assembly of the fungal hydrophobins.
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Analysis of the structure and conformational states of DewA gives insight into the assembly of the fungal hydrophobins.

机译：通过对DewA的结构和构象状态进行分析，可以深入了解真菌疏水蛋白的组装过程。

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摘要

The hydrophobin DewA from the fungus Aspergillus nidulans is a highly surface-active protein that spontaneously self-assembles into amphipathic monolayers at hydrophobic:hydrophilic interfaces. These monolayers are composed of fibrils that are a form of functional amyloid. While there has been significant interest in the use of DewA for a variety of surface coatings and as an emulsifier in biotechnological applications, little is understood about the structure of the protein or the mechanism of self-assembly. We have solved the solution NMR structure of DewA. While the pattern of four disulfide bonds that is a defining feature of hydrophobins is conserved, the arrangement and composition of secondary-structure elements in DewA are quite different to what has been observed in other hydrophobin structures. In addition, we demonstrate that DewA populates two conformations in solution, both of which are assembly competent. One conformer forms a dimer at high concentrations, but this dimer is off-pathway to fibril formation and may represent an assembly control mechanism. These data highlight the structural differences between fibril-forming hydrophobins and those that form amorphous monolayers. This work will open up new opportunities for the engineering of hydrophobins with novel biotechnological applications.
机译：来自构巢曲霉（Aspergillus nidulans）的疏水蛋白DewA是一种高度表面活性的蛋白，可在疏水：亲水界面自发自组装成两亲性单分子膜。这些单层由功能性淀粉样蛋白形式的原纤维组成。尽管人们对将DewA用于各种表面涂料以及作为生物技术应用中的乳化剂引起了极大的兴趣，但对蛋白质的结构或自组装机制了解甚少。我们已经解决了DewA的溶液NMR结构。虽然保留了作为疏水蛋白的主要特征的四个二硫键的模式，但DewA中二级结构元素的排列和组成与在其他疏水蛋白结构中观察到的完全不同。此外，我们证明了DewA在溶液中填充了两个构象，这两个构象都可以组装。一个构象异构体在高浓度下会形成一个二聚体，但是该二聚体不参与原纤维形成，可能代表了组装控制机制。这些数据突出了原纤维形成的疏水蛋白与形成非晶单层的疏水蛋白之间的结构差异。这项工作将为具有新型生物技术应用的疏水蛋白工程开辟新的机会。

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