2nbh: Difference between revisions
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<StructureSection load='2nbh' size='340' side='right'caption='[[2nbh]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2nbh' size='340' side='right'caption='[[2nbh]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2nbh]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2nbh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schcm Schcm]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NBH FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HYD1, SCHCODRAFT_58269 ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HYD1, SCHCODRAFT_58269 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=578458 SCHCM])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nbh OCA], [https://pdbe.org/2nbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nbh RCSB], [https://www.ebi.ac.uk/pdbsum/2nbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nbh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> |
Revision as of 19:37, 6 July 2022
Solution structure of the HYD1 hydrophobin from Schizophyllum communeSolution structure of the HYD1 hydrophobin from Schizophyllum commune
Structural highlights
Publication Abstract from PubMedClass I hydrophobins are functional amyloids secreted by fungi. They self-assemble into organized films at interfaces producing structures that include cellular adhesion points and hydrophobic coatings. Here, we present the first structure and solution properties of a unique Class I protein sequence of Basidiomycota origin: the Schizophyllum commune hydrophobin SC16 (hyd1). While the core beta-barrel structure and disulphide bridging characteristic of the hydrophobin family are conserved, its surface properties and secondary structure elements are reminiscent of both Class I and II hydrophobins. Sequence analyses of hydrophobins from 215 fungal species suggest this structure is largely applicable to a high-identity Basidiomycota Class I subdivision (IB). To validate this prediction, structural analysis of a comparatively distinct Class IB sequence from a different fungal order, namely the Phanerochaete carnosa PcaHyd1, indicates secondary structure properties similar to that of SC16. Together, these results form an experimental basis for a high-identity Class I subdivision and contribute to our understanding of functional amyloid formation. Characterization of a Basidiomycota hydrophobin reveals the structural basis for a high-similarity Class I subdivision.,Gandier JA, Langelaan DN, Won A, O'Donnell K, Grondin JL, Spencer HL, Wong P, Tillier E, Yip C, Smith SP, Master ER Sci Rep. 2017 Apr 10;7:45863. doi: 10.1038/srep45863. PMID:28393921[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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