View source for 2lsh


==Solution structure of the class I hydrophobin DewA==
<StructureSection load='2lsh' size='340' side='right'caption='[[2lsh]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lsh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_nidulans_FGSC_A4 Aspergillus nidulans FGSC A4]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LSH 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=2lsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lsh OCA], [https://pdbe.org/2lsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lsh RCSB], [https://www.ebi.ac.uk/pdbsum/2lsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lsh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DEWA_EMENI DEWA_EMENI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The hydrophobin DewA from the fungus Aspergillus nidulans is a highly surface-active protein that spontaneously self-assembles into amphipathic monolayers at hydrophobic:hydrophilic interfaces. These monolayers are composed of fibrils that are a form of functional amyloid. While there has been significant interest in the use of DewA for a variety of surface coatings and as an emulsifier in biotechnological applications, little is understood about the structure of the protein or the mechanism of self-assembly. We have solved the solution NMR structure of DewA. While the pattern of four disulfide bonds that is a defining feature of hydrophobins is conserved, the arrangement and composition of secondary-structure elements in DewA are quite different to what has been observed in other hydrophobin structures. In addition, we demonstrate that DewA populates two conformations in solution, both of which are assembly competent. One conformer forms a dimer at high concentrations, but this dimer is off-pathway to fibril formation and may represent an assembly control mechanism. These data highlight the structural differences between fibril-forming hydrophobins and those that form amorphous monolayers. This work will open up new opportunities for the engineering of hydrophobins with novel biotechnological applications.

Analysis of the Structure and Conformational States of DewA Gives Insight into the Assembly of the Fungal Hydrophobins.,Morris VK, Kwan AH, Sunde M J Mol Biol. 2012 Nov 5. pii: S0022-2836(12)00854-6. doi:, 10.1016/j.jmb.2012.10.021. PMID:23137797<ref>PMID:23137797</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lsh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Aspergillus nidulans FGSC A4]]
[[Category: Large Structures]]
[[Category: Kwan AH]]
[[Category: Mackay JP]]
[[Category: Morris VK]]
[[Category: Sunde M]]