Structural highlights
Function
[HYP2_TRIRE] Responsible for spore hydrophobicity and protection.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Hydrophobins are small proteins secreted by filamentous fungi that have a unique ability to spontaneously form amphiphilic layers. Hydrophobins have only recently been structurally characterized through the first crystal structure determination of a protein of this class, Trichoderma reesei hydrophobin HFBII [Hakanpaa, Paananen et al. (2004), J. Biol. Chem. 279, 534-539]. The resolution of the HFBII structure has now been extended to an ultrahigh resolution of 0.75 A. The structure was refined conventionally and multipole refinement has been initiated. The ultrahigh-resolution structure is analyzed here in detail and comparison is made to the previous atomic resolution structure of the same protein as well as to other ultrahigh-resolution structures found in the Protein Data Bank.
Hydrophobin HFBII in detail: ultrahigh-resolution structure at 0.75 A.,Hakanpaa J, Linder M, Popov A, Schmidt A, Rouvinen J Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):356-67. Epub 2006, Mar 18. PMID:16552136[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hakanpaa J, Linder M, Popov A, Schmidt A, Rouvinen J. Hydrophobin HFBII in detail: ultrahigh-resolution structure at 0.75 A. Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):356-67. Epub 2006, Mar 18. PMID:16552136 doi:http://dx.doi.org/10.1107/S0907444906000862
