2b97 | pdb_00002b97

Ultra-high resolution structure of hydrophobin HFBII

spinqualitylabelsall models 2b97, resolution 0.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2b97 is a 2 chain structure with sequence from Trichoderma reesei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MN Related: 1r2m Resources: FirstGlance, OCA, RCSB, PDBsum Function [HYP2_TRIRE] Responsible for spore hydrophobicity and protection. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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