ArticleProceedings of the National Academy of Sciences of the United States of America2006
Structural basis for rodlet assembly in fungal hydrophobins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
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Who cites it
86 citing papers in PubMed.
- Characterization of the Polysaccharide and Protein Composition ofJournal of fungi (Basel, Switzerland) · 2026Article
- Amorphous-to-rodlet structural transition governs the interfacial functions ofFrontiers in microbiology · 2026Article
- Hydrophobins RolA and HypB fromMycoscience · 2026Article
- AlphaFold modeling uncovers global structural features of class I and class II fungal hydrophobins.Protein science : a publication of the Protein Society · 2025Article
- Structural elucidation of four fungal hydrophobins belonging to classes I and II: Results from Alphafold and accelerated molecular dynamics simulations.Computational and structural biotechnology journal · 2025Article
- Design of Plastic Binding Lytic Polysaccharide Monooxygenases via Modular Engineering.Chem & bio engineering · 2024Article
- Protein disulfide isomerase 1 is required for RodA assembling-based conidial hydrophobicity ofApplied and environmental microbiology · 2024Article
- Identification and Characterization of a Predominant Hydrophobin in the Edible MushroomJournal of fungi (Basel, Switzerland) · 2023Article
- Protein-Based Biological Materials: Molecular Design and Artificial Production.Chemical reviews · 2023Review
- Structural and Functional Annotation of Hypothetical Proteins from the Microsporidia SpeciesInternational journal of molecular sciences · 2023Article
- Characterization of the structure and self-assembly of two distinct class IB hydrophobins.Applied microbiology and biotechnology · 2022Article
- TheJournal of fungi (Basel, Switzerland) · 2022Article
- Identification of Candidate Ice Nucleation Activity (INA) Genes inJournal of fungi (Basel, Switzerland) · 2022Article
- What makes functional amyloids work?Critical reviews in biochemistry and molecular biology · 2022Review
- Review
- Reshaping sub-millimetre bubbles from spheres to tori.Soft matter · 2022Article
- Adsorption Kinetics and Self-Assembled Structures of Aspergillus oryzae Hydrophobin RolA on Hydrophobic and Charged Solid Surfaces.Applied and environmental microbiology · 2022Article
- The N-terminal tail of the hydrophobin SC16 is not required for rodlet formation.Scientific reports · 2022Article
- Emerging prospects of protein/peptide-based nanoassemblies for drug delivery and vaccine development.Nano research · 2022Article
- A novel hydrophobin encoded byFrontiers in microbiology · 2022Article
26 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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