2LFN

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

Summary for 2LFN

• Entry DOI: 10.2210/pdb2lfn/pdb
• Related: 2FMC 2K6A
• NMR Information: BMRB: 17765
• Descriptor: Hydrophobin (1 entity in total)
• Functional Keywords: surface active protein, protein self-assembly, hydrophobin, fungal protein, structural protein
• Biological source: Neurospora crassa
• Cellular location: Secreted, cell wall: Q04571
• Total number of polymer chains: 1
• Total formula weight: 6728.58

Authors

Macindoe, I.,Kwan, A.H.,Morris, V.K.,Mackay, J.P.,Sunde, M. (deposition date: 2011-07-06, release date: 2012-01-25, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

SOLUTION NMR