Hydrophobin
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| Structure of hydrophobin HFBI from Trichoderma reesei | ||
| Fungal hydrophobin | ||
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| Identifiers | ||
| Symbol | Hydrophobin_2 | |
| Pfam | PF06766 | |
| InterPro | IPR010636 | |
| PROSITE | PDOC00739 | |
| SCOP | 1r2m | |
| OPM protein | 1r2m | |
| Available PDB structures:
1r2mB:17-82 |
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Hydrophobins are a class of small, cysteine rich proteins (~ 100 amino acids) that are expressed only by filamentousfungi (ascomycetes and basidiomycetes). They are known for their capability of forming a water-insoluble coating on a surface of an object. They were first discovered and separated in Schizophyllum commune in 1991. Based on differences in hydropathy patterns and biophysical properties, they are divided into two categories:class I and class II.
Fungi make complex aerial structures and spores even in aqueous environments. Hydrophobins coat the spores which means they do not clog together.
The fungal hydrophobins seem to be restricted to ascomycetes. Hydrophobins are generally found on the outer surface of conidia and of the hyphal wall, and may be involved in mediating contact and communication between the fungus and its environment[1]. Some family members contain multiple copies of the domain.
[edit] References
- ^ Whiteford JR, Spanu PD (2001). "The hydrophobin HCf-1 of Cladosporium fulvum is required for efficient water-mediated dispersal of conidia". Fungal Genet. Biol. 32 (3): 159–168. doi:. PMID 11343402.
[edit] Further reading
- Scholtmeijer, Karin (2000). "Expression and engineering of hydrophobin genes". . University of Groningen
- J. Hakanpää, A. Paananen, S. Askolin, T. Nakari-Setälä, T. Parkkinen, M. Penttilä, M. B. Linder, J. Rouvinen (2004). "Atomic Resolution Structure of the HFBII Hydrophobin, a Self-assembling Amphiphile". The Journal of Biological Chemistry 279 (1): 534–539. doi:.
- H. A. B. Wösten, M. L. de Vocht (2000). "Hydrophobins, the fungal coat unravelled". Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes 1469 (2): 79–86. doi:.
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