2b97
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(New page: 200px<br /><applet load="2b97" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b97, resolution 0.75Å" /> '''Ultra-high resolutio...)
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Revision as of 06:31, 21 November 2007
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Ultra-high resolution structure of hydrophobin HFBII
Overview
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 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.
About this Structure
2B97 is a Single protein structure of sequence from Hypocrea jecorina with MN as ligand. Full crystallographic information is available from OCA.
Reference
Hydrophobin HFBII in detail: ultrahigh-resolution structure at 0.75 A., Hakanpaa J, Linder M, Popov A, Schmidt A, Rouvinen J, Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):356-67. Epub 2006, Mar 18. PMID:16552136
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