2lsh

Solution structure of the class I hydrophobin DewA

spinqualitylabelsall models 2lsh Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lsh is a 1 chain structure with sequence from Aspergillus nidulans FGSC A4. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DEWA_EMENI Publication Abstract from PubMed The hydrophobin DewA from the fungus Aspergillus nidulans is a highly surface-active protein that spontaneously self-assembles into amphipathic monolayers at hydrophobic:hydrophilic interfaces. These monolayers are composed of fibrils that are a form of functional amyloid. While there has been significant interest in the use of DewA for a variety of surface coatings and as an emulsifier in biotechnological applications, little is understood about the structure of the protein or the mechanism of self-assembly. We have solved the solution NMR structure of DewA. While the pattern of four disulfide bonds that is a defining feature of hydrophobins is conserved, the arrangement and composition of secondary-structure elements in DewA are quite different to what has been observed in other hydrophobin structures. In addition, we demonstrate that DewA populates two conformations in solution, both of which are assembly competent. One conformer forms a dimer at high concentrations, but this dimer is off-pathway to fibril formation and may represent an assembly control mechanism. These data highlight the structural differences between fibril-forming hydrophobins and those that form amorphous monolayers. This work will open up new opportunities for the engineering of hydrophobins with novel biotechnological applications. Analysis of the Structure and Conformational States of DewA Gives Insight into the Assembly of the Fungal Hydrophobins.,Morris VK, Kwan AH, Sunde M J Mol Biol. 2012 Nov 5. pii: S0022-2836(12)00854-6. doi:, 10.1016/j.jmb.2012.10.021. PMID:23137797 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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