6gcj

Solution structure of the RodA hydrophobin from Aspergillus fumigatus

spinqualitylabelsall models 6gcj, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6gcj is a 1 chain structure with sequence from Aspfc. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: AFUB_057130 (ASPFC) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Hydrophobins are fungal proteins characterised by their amphipathic properties and an idiosyncratic pattern of eight cysteine residues involved in four disulphide bridges. The soluble form of these proteins spontaneously self-assembles at hydrophobic/hydrophilic interfaces to form an amphipathic monolayer. The RodA hydrophobin of the opportunistic pathogen Aspergillus fumigatus forms an amyloid layer with a rodlet morphology that covers the surface of fungal spores. This rodlet layer bestows hydrophobicity to the spores facilitating their dispersal in the air and rendering the conidia inert relative to the human immune system. As a first step in the analysis of the solution structure and self-association of RodA, we report the (1)H, (13)C and (15)N resonance assignments of the soluble monomeric form of RodA. (1)H, (13)C and (15)N resonance assignments of the RodA hydrophobin from the opportunistic pathogen Aspergillus fumigatus.,Pille A, Kwan AH, Cheung I, Hampsey M, Aimanianda V, Delepierre M, Latge JP, Sunde M, Guijarro JI Biomol NMR Assign. 2015 Apr;9(1):113-8. doi: 10.1007/s12104-014-9555-1. PMID:24659460 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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