2B97

Ultra-high resolution structure of hydrophobin HFBII

Summary for 2B97

• Entry DOI: 10.2210/pdb2b97/pdb
• Related: 1R2M
• Descriptor: Hydrophobin II, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: hydrophobin, surfactant, amphiphilic, surface active protein
• Biological source: Hypocrea jecorina
• Cellular location: Spore wall: P79073
• Total number of polymer chains: 2
• Total formula weight: 14457.89

Authors

Hakanpaa, J.,Linder, M.,Popov, A.,Schmidt, A.,Rouvinen, J. (deposition date: 2005-10-11, release date: 2006-03-28, Last modification date: 2024-10-16)

Primary citation

Hakanpaa, J.,Linder, M.,Popov, A.,Schmidt, A.,Rouvinen, J.
Hydrophobin HFBII in detail: ultrahigh-resolution structure at 0.75 A.
Acta Crystallogr.,Sect.D, 62:356-367, 2006

PubMed 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 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.

PubMed: 16552136
DOI: 10.1107/S0907444906000862

Experimental method

X-RAY DIFFRACTION (0.75 Å)