4n6q
From Proteopedia
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| - | + | ==Crystal structure of VosA velvet domain== | |
| - | === | + | <StructureSection load='4n6q' size='340' side='right' caption='[[4n6q]], [[Resolution|resolution]] 1.79Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4n6q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/A._nidulans A. nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N6Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N6Q FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n6r|4n6r]]</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=4n6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n6q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n6q RCSB], [http://www.ebi.ac.uk/pdbsum/4n6q PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Morphological development of fungi and their combined production of secondary metabolites are both acting in defence and protection. These processes are mainly coordinated by velvet regulators, which contain a yet functionally and structurally uncharacterized velvet domain. Here we demonstrate that the velvet domain of VosA is a novel DNA-binding motif that specifically recognizes an 11-nucleotide consensus sequence consisting of two motifs in the promoters of key developmental regulatory genes. The crystal structure analysis of the VosA velvet domain revealed an unforeseen structural similarity with the Rel homology domain (RHD) of the mammalian transcription factor NF-kappaB. Based on this structural similarity several conserved amino acid residues present in all velvet domains have been identified and shown to be essential for the DNA binding ability of VosA. The velvet domain is also involved in dimer formation as seen in the solved crystal structures of the VosA homodimer and the VosA-VelB heterodimer. These findings suggest that defence mechanisms of both fungi and animals might be governed by structurally related DNA-binding transcription factors. | ||
| - | + | The Velvet Family of Fungal Regulators Contains a DNA-Binding Domain Structurally Similar to NF-kappaB.,Ahmed YL, Gerke J, Park HS, Bayram O, Neumann P, Ni M, Dickmanns A, Kim SC, Yu JH, Braus GH, Ficner R PLoS Biol. 2013 Dec;11(12):e1001750. doi: 10.1371/journal.pbio.1001750. Epub 2013, Dec 31. PMID:24391470<ref>PMID:24391470</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Ahmed, Y L | + | == References == |
| - | [[Category: Dickmanns, A | + | <references/> |
| - | [[Category: Ficner, R | + | __TOC__ |
| - | [[Category: Neumann, P | + | </StructureSection> |
| + | [[Category: A. nidulans]] | ||
| + | [[Category: Ahmed, Y L]] | ||
| + | [[Category: Dickmanns, A]] | ||
| + | [[Category: Ficner, R]] | ||
| + | [[Category: Neumann, P]] | ||
[[Category: Beta-sandwich]] | [[Category: Beta-sandwich]] | ||
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
Revision as of 18:46, 21 December 2014
Crystal structure of VosA velvet domain
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