(1)H, (13)C and (15)N resonance assignments of the RodA hydrophobin from the opportunistic pathogen Aspergillus fumigatus.

Abstract:

: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.

journal_name

Biomol NMR Assign

authors

Pille A,Kwan AH,Cheung I,Hampsey M,Aimanianda V,Delepierre M,Latge JP,Sunde M,Guijarro JI

doi

10.1007/s12104-014-9555-1

subject

Has Abstract

pub_date

2015-04-01 00:00:00

pages

113-8

issue

1

eissn

1874-2718

issn

1874-270X

journal_volume

9

pub_type

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