4aog

Solution structure of the Class II hydrophobin NC2

spinqualitylabelsall models 4aog, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4aog is a 1 chain structure with sequence from Neucr. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Hydrophobins are fungal proteins that self-assemble spontaneously to form amphipathic monolayers at hydrophobic:hydrophilic interfaces. Hydrophobin assemblies facilitate fungal transitions between wet and dry environments and interactions with plant and animal hosts. NC2 is a previously uncharacterised hydrophobin from Neurospora crassa. It is a highly surface active protein and is able to form protein layers on a water:air interface that stabilise air bubbles. On a hydrophobic substrate, NC2 forms layers consisting of an ordered network of protein molecules which dramatically decrease the water contact angle. The solution structure and dynamics of NC2 have been determined using nuclear magnetic resonance spectroscopy. The structure of this protein displays the same core fold as observed in other hydrophobin structures determined to date, including the class II hydrophobins HFBI and HFBII from Trichoderma reesei, but certain features illuminate the structural differences between class I and class II hydrophobins and also highlight the variations between structures of class II hydrophobin family members. The unique properties of hydrophobins have attracted much attention for biotechnology applications. The insights obtained through determining the structure, biophysical properties and assembly characteristics of NC2 will facilitate the development of hydrophobin-based applications. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc. Solution structure and interface-driven self-assembly of NC2, a new member of the class II hydrophobin proteins.,Ren Q, Kwan AH, Sunde M Proteins. 2013 Nov 12. doi: 10.1002/prot.24473. PMID:24218020 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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