Download MendeleyHydrophobin HFBII in detail: ultrahigh-resolution structure at 0.75 A.
Hakanpaa, J., Linder, M., Popov, A., Schmidt, A., Rouvinen, J.(2006) Acta Crystallogr D Biol Crystallogr 62: 356-367
- PubMed: 16552136
- DOI: https://doi.org/10.1107/S0907444906000862
- Primary Citation of Related Structures:
2B97 - PubMed Abstract:
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 [Hakanpää, 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.
Organizational Affiliation:
Department of Chemistry, University of Joensuu, PO Box 111, 80101 Joensuu, Finland. johanna.hakanpaa@joensuu.fi
