2FMC

Solution structure of the class I hydrophobin EAS

2FMC の概要

• エントリーDOI: 10.2210/pdb2fmc/pdb
• 関連するPDBエントリー: 1R2M
• 分子名称: Hydrophobin (1 entity in total)
• 機能のキーワード: beta barrel, flexible loop, disulphide bonds, surface active protein
• 由来する生物種: Neurospora crassa
• 細胞内の位置: Secreted, cell wall: Q04571
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8189.34

構造登録者

Kwan, A.H. (登録日: 2006-01-09, 公開日: 2006-03-28, 最終更新日: 2024-10-23)

主引用文献

Kwan, A.H.,Winefield, R.D.,Sunde, M.,Matthews, J.M.,Haverkamp, R.G.,Templeton, M.D.,Mackay, J.P.
Structural basis for rodlet assembly in fungal hydrophobins
Proc.Natl.Acad.Sci.Usa, 103:3621-3626, 2006

PubMed Abstract: Class I hydrophobins are a unique family of fungal proteins that form a polymeric, water-repellent monolayer on the surface of structures such as spores and fruiting bodies. Similar monolayers are being discovered on an increasing range of important microorganisms. Hydrophobin monolayers are amphipathic and particularly robust, and they reverse the wettability of the surface on which they are formed. There are also significant similarities between these polymers and amyloid-like fibrils. However, structural information on these proteins and the rodlets they form has been elusive. Here, we describe the three-dimensional structure of the monomeric form of the class I hydrophobin EAS. EAS forms a beta-barrel structure punctuated by several disordered regions and displays a complete segregation of charged and hydrophobic residues on its surface. This structure is consistent with its ability to form an amphipathic polymer. By using this structure, together with data from mutagenesis and previous biophysical studies, we have been able to propose a model for the polymeric rodlet structure adopted by these proteins. X-ray fiber diffraction data from EAS rodlets are consistent with our model. Our data provide molecular insight into the nature of hydrophobin rodlet films and extend our understanding of the fibrillar beta-structures that continue to be discovered in the protein world.

PubMed: 16537446
DOI: 10.1073/pnas.0505704103

実験手法

SOLUTION NMR