Hakanpää Johanna, Linder Markus, Popov Alexander, Schmidt Andrea, Rouvinen Juha
Department of Chemistry, University of Joensuu, PO Box 111, 80101 Joensuu, Finland.
Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):356-67. doi: 10.1107/S0907444906000862. Epub 2006 Mar 18.
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.
疏水蛋白是丝状真菌分泌的小蛋白，具有自发形成两亲层的独特能力。直到最近，通过对这类蛋白中的里氏木霉疏水蛋白HFBII进行首次晶体结构测定，疏水蛋白的结构才得以表征[哈坎佩、帕纳宁等人（2004年），《生物化学杂志》279卷，534 - 539页]。现在，HFBII结构的分辨率已扩展至0.75埃的超高分辨率。该结构按常规方法进行了精修，并且已启动多极精修。在此详细分析超高分辨率结构，并将其与同一蛋白先前的原子分辨率结构以及蛋白质数据库中发现的其他超高分辨率结构进行比较。
