2LFN

Identification of the key regions that drive functional amyloid formation by the fungal hydrophobin EAS

2LFN の概要

• エントリーDOI: 10.2210/pdb2lfn/pdb
• 関連するPDBエントリー: 2FMC 2K6A
• NMR情報: BMRB: 17765
• 分子名称: Hydrophobin (1 entity in total)
• 機能のキーワード: surface active protein, protein self-assembly, hydrophobin, fungal protein, structural 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: 6728.58

構造登録者

Macindoe, I.,Kwan, A.H.,Morris, V.K.,Mackay, J.P.,Sunde, M. (登録日: 2011-07-06, 公開日: 2012-01-25, 最終更新日: 2024-10-30)

主引用文献

Macindoe, I.,Kwan, A.H.,Ren, Q.,Morris, V.K.,Yang, W.,Mackay, J.P.,Sunde, M.
Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS
Proc.Natl.Acad.Sci.USA, 109:E804-E811, 2012

PubMed Abstract: The hydrophobin EAS from the fungus Neurospora crassa forms functional amyloid fibrils called rodlets that facilitate spore formation and dispersal. Self-assembly of EAS into fibrillar rodlets occurs spontaneously at hydrophobic:hydrophilic interfaces and the rodlets further associate laterally to form amphipathic monolayers. We have used site-directed mutagenesis and peptide experiments to identify the region of EAS that drives intermolecular association and formation of the cross-β rodlet structure. Transplanting this region into a nonamyloidogenic hydrophobin enables it to form rodlets. We have also determined the structure and dynamics of an EAS variant with reduced rodlet-forming ability. Taken together, these data allow us to pinpoint the conformational changes that take place when hydrophobins self-assemble at an interface and to propose a model for the amphipathic EAS rodlet structure.

PubMed: 22308366
DOI: 10.1073/pnas.1114052109

実験手法

SOLUTION NMR