Hydrophobin HFBII in detail: ultrahigh-resolution structure at 0.75 A.
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.
Hakanpää
Johanna
J
Department of Chemistry, University of Joensuu, PO Box 111, 80101 Joensuu, Finland. johanna.hakanpaa@joensuu.fi
Linder
Markus
M
Popov
Alexander
A
Schmidt
Andrea
A
Rouvinen
Juha
J
D016880:Anisotropy; D003460:Crystallization; D018360:Crystallography, X-Ray; D003553:Cystine / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry*; D006859:Hydrogen / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D008345:Manganese / Q000737:chemistry; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D055672:Static Electricity; D013499:Surface Properties; D014242:Trichoderma / Q000737:chemistry*; D014867:Water / Q000737:chemistry
D005656:Fungal Proteins; D014867:Water; D008345:Manganese; D003553:Cystine; D006859:Hydrogen