Hydrophobin HFBII in detail:: ultrahigh-resolution structure at 0.75 Å

被引:79
作者
Hakanpää, J
Linder, M
Popov, A
Schmidt, A
Rouvinen, J
机构
[1] Univ Joensuu, Dept Chem, FIN-80101 Joensuu, Finland
[2] VTT Biotechnol, Espoo 02044, Finland
[3] EMBL Hamburg, DESY, D-22603 Hamburg, Germany
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2006年 / 62卷
关键词
D O I
10.1107/S0907444906000862
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 angstrom. 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.
引用
收藏
页码:356 / 367
页数:12
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