2kcn: Difference between revisions
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<StructureSection load='2kcn' size='340' side='right' caption='[[2kcn]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2kcn' size='340' side='right' caption='[[2kcn]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2kcn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2kcn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_306.48 Cbs 306.48]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KCN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KCN FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">paf ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5076 | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">paf ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5076 CBS 306.48])</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=2kcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kcn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kcn RCSB], [http://www.ebi.ac.uk/pdbsum/2kcn PDBsum]</span></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=2kcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kcn OCA], [http://pdbe.org/2kcn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kcn RCSB], [http://www.ebi.ac.uk/pdbsum/2kcn PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2kcn" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Cbs 306 48]] | ||
[[Category: Barna, T]] | [[Category: Barna, T]] | ||
[[Category: Batta, G]] | [[Category: Batta, G]] | ||
Revision as of 22:09, 10 September 2015
Solution structure of the antifungal protein PAF from Penicillium chrysogenumSolution structure of the antifungal protein PAF from Penicillium chrysogenum
Structural highlights
Publication Abstract from PubMedPenicillium antifungal protein (PAF) is a promising antimycotic without toxic effects on mammalian cells and therefore may represent a drug candidate against the often lethal Aspergillus infections that occur in humans. The pathogenesis of PAF on sensitive fungi involves G-protein coupled signalling followed by apoptosis. In the present study, the solution structure of this small, cationic, antifungal protein from Penicillium chrysogenum is determined by NMR. We demonstrate that PAF belongs to the structural classification of proteins fold class of its closest homologue antifungal protein from Aspergillus giganteus. PAF comprises five beta-strands forming two orthogonally packed beta-sheets that share a common interface. The ambiguity in the assignment of two disulfide bonds out of three was investigated by NMR dynamics, together with restrained molecular dynamics calculations. The clue could not be resolved: the two ensembles with different disulfide patterns and the one with no S-S bond exhibit essentially the same fold. (15)N relaxation dispersion and interference experiments did not reveal disulfide bond rearrangements via slow exchange. The measured order parameters and the 3.0 ns correlation time are appropriate for a compact monomeric protein of this size. Using site-directed mutagenesis, we demonstrate that the highly-conserved and positively-charged lysine-rich surface region enhances the toxicity of PAF. However, the binding capability of the oligosaccharide/oligonucleotide binding fold is reduced in PAF compared to antifungal protein as a result of less solvent-exposed aromatic regions, thus explaining the absence of chitobiose binding. The present study lends further support to the understanding of the documented substantial differences between the mode of action of two highly homologous antifungal proteins. Functional aspects of the solution structure and dynamics of PAF--a highly-stable antifungal protein from Penicillium chrysogenum.,Batta G, Barna T, Gaspari Z, Sandor S, Kover KE, Binder U, Sarg B, Kaiserer L, Chhillar AK, Eigentler A, Leiter E, Hegedus N, Pocsi I, Lindner H, Marx F FEBS J. 2009 May;276(10):2875-90. PMID:19459942[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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