View source for 2lfn


==Identification of the key regions that drive functional amyloid formation by the fungal hydrophobin EAS==
<StructureSection load='2lfn' size='340' side='right'caption='[[2lfn]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lfn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa_OR74A Neurospora crassa OR74A]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LFN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lfn OCA], [https://pdbe.org/2lfn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lfn RCSB], [https://www.ebi.ac.uk/pdbsum/2lfn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lfn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RODL_NEUCR RODL_NEUCR] Contributes to surface hydrophobicity, which is important for processes such as association of hyphae in reproductive structures, dispersal of aerial spores and adhesion of pathogens to host structures. Important for the formation of hydrophobic rodlet layers of asexually-produced spores.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The hydrophobin EAS from the fungus Neurospora crassa forms functional amyloid fibrils called rodlets that facilitate spore formation and dispersal. Self-assembly of EAS into fibrillar rodlets occurs spontaneously at hydrophobic:hydrophilic interfaces and the rodlets further associate laterally to form amphipathic monolayers. We have used site-directed mutagenesis and peptide experiments to identify the region of EAS that drives intermolecular association and formation of the cross-beta rodlet structure. Transplanting this region into a nonamyloidogenic hydrophobin enables it to form rodlets. We have also determined the structure and dynamics of an EAS variant with reduced rodlet-forming ability. Taken together, these data allow us to pinpoint the conformational changes that take place when hydrophobins self-assemble at an interface and to propose a model for the amphipathic EAS rodlet structure.

Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS.,Macindoe I, Kwan AH, Ren Q, Morris VK, Yang W, Mackay JP, Sunde M Proc Natl Acad Sci U S A. 2012 Apr 3;109(14):E804-11. Epub 2012 Jan 23. PMID:22308366<ref>PMID:22308366</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lfn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Neurospora crassa OR74A]]
[[Category: Kwan AH]]
[[Category: Macindoe I]]
[[Category: Mackay JP]]
[[Category: Morris VK]]
[[Category: Sunde M]]