Hydrophobin HFBII in detail

Ultrahigh-resolution structure at 0.75 Å

J. Hakanpää, Markus Linder, A. Popov, A. Schmidt, Juha Rouvinen

Research output: Contribution to journalArticleScientificpeer-review

73 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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Keywords

  • proteins
  • hydrophobins
  • filamentous fungi
  • Trichoderma reesei
  • crystallization

Cite this

Hakanpää, J. ; Linder, Markus ; Popov, A. ; Schmidt, A. ; Rouvinen, Juha. / Hydrophobin HFBII in detail : Ultrahigh-resolution structure at 0.75 Å. In: Acta Crystallographica Section D: Biological Crystallography. 2006 ; Vol. 62, No. 4. pp. 356-367.
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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 [Hakanp{\"a}{\"a}, 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 {\AA}. 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.",
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Hydrophobin HFBII in detail : Ultrahigh-resolution structure at 0.75 Å. / Hakanpää, J.; Linder, Markus; Popov, A.; Schmidt, A.; Rouvinen, Juha.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 62, No. 4, 2006, p. 356-367.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Hydrophobin HFBII in detail

T2 - Ultrahigh-resolution structure at 0.75 Å

AU - Hakanpää, J.

AU - Linder, Markus

AU - Popov, A.

AU - Schmidt, A.

AU - Rouvinen, Juha

PY - 2006

Y1 - 2006

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AB - 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.

KW - proteins

KW - hydrophobins

KW - filamentous fungi

KW - Trichoderma reesei

KW - crystallization

U2 - 10.1107/S0907444906000862

DO - 10.1107/S0907444906000862

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JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

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