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

Johanna Hakanpää*, Markus Linder, Alexander Popov, Andrea Schmidt, Juha Rouvinen

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

80 Citations (Scopus)

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 Å. 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.

Original languageEnglish
Pages (from-to)356-367
Number of pages12
JournalACTA CRYSTALLOGRAPHICA SECTION D : BIOLOGICAL CRYSTALLOGRAPHY
Volume62
Issue number4
DOIs
Publication statusPublished - 2006
MoE publication typeA1 Journal article-refereed

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