View source for 6gcj


==Solution structure of the RodA hydrophobin from Aspergillus fumigatus==
<StructureSection load='6gcj' size='340' side='right'caption='[[6gcj]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6gcj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfc Aspfc]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GCJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GCJ FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AFUB_057130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=451804 ASPFC])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gcj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gcj OCA], [http://pdbe.org/6gcj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gcj RCSB], [http://www.ebi.ac.uk/pdbsum/6gcj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gcj ProSAT]</span></td></tr>
</table>
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== 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<ref>PMID:24659460</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspfc]]
[[Category: Large Structures]]
[[Category: Aimanianda, V]]
[[Category: Guijarro, J I]]
[[Category: Kwan, A]]
[[Category: Latge, J P]]
[[Category: Pille, A]]
[[Category: Sunde, M]]
[[Category: Soluble form of the protein that coats aspergillus fumigatus conidia]]
[[Category: Structural protein]]