4n6r

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of VosA-VelB-complex

Structural highlights

4n6r is a 2 chain structure with sequence from Aspergillus nidulans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VOSA_EMENI Component of the velB-VosA heterodimeric complex that plays a dual role in activating genes associated with spore maturation and repressing certain development-associated genes (PubMed:17912349, PubMed:21152013, PubMed:23049895, PubMed:24391470). Controls primarily the late process of sporulation including trehalose biogenesis (PubMed:17912349). The complex binds DNA through the DNA-binding domain of vosA that recognizes an 11-nucleotide consensus sequence 5'-CTGGCCGCGGC-3' consisting of two motifs in the promoters of key developmental regulatory genes (PubMed:24391470). The vosA-velB complex binds to the beta-glucan synthase fksA gene promoter in asexual spores for repression (PubMed:25960370).[UniProtKB:A0SP16]^[1] ^[2] ^[3] ^[4]

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ni M, Yu JH. A novel regulator couples sporogenesis and trehalose biogenesis in Aspergillus nidulans. PLoS One. 2007 Oct 3;2(10):e970. doi: 10.1371/journal.pone.0000970. PMID:17912349 doi:http://dx.doi.org/10.1371/journal.pone.0000970
↑ Sarikaya Bayram O, Bayram O, Valerius O, Park HS, Irniger S, Gerke J, Ni M, Han KH, Yu JH, Braus GH. LaeA control of velvet family regulatory proteins for light-dependent development and fungal cell-type specificity. PLoS Genet. 2010 Dec 2;6(12):e1001226. doi: 10.1371/journal.pgen.1001226. PMID:21152013 doi:http://dx.doi.org/10.1371/journal.pgen.1001226
↑ Park HS, Ni M, Jeong KC, Kim YH, Yu JH. The role, interaction and regulation of the velvet regulator VelB in Aspergillus nidulans. PLoS One. 2012;7(9):e45935. doi: 10.1371/journal.pone.0045935. Epub 2012 Sep 25. PMID:23049895 doi:http://dx.doi.org/10.1371/journal.pone.0045935
↑ Park HS, Man Yu Y, Lee MK, Jae Maeng P, Chang Kim S, Yu JH. Velvet-mediated repression of beta-glucan synthesis in Aspergillus nidulans spores. Sci Rep. 2015 May 11;5:10199. doi: 10.1038/srep10199. PMID:25960370 doi:http://dx.doi.org/10.1038/srep10199
↑ Ahmed YL, Gerke J, Park HS, Bayram O, Neumann P, Ni M, Dickmanns A, Kim SC, Yu JH, Braus GH, Ficner R. The Velvet Family of Fungal Regulators Contains a DNA-Binding Domain Structurally Similar to NF-kappaB. PLoS Biol. 2013 Dec;11(12):e1001750. doi: 10.1371/journal.pbio.1001750. Epub 2013, Dec 31. PMID:24391470 doi:http://dx.doi.org/10.1371/journal.pbio.1001750

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4n6r"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4n6r is ON HOLD
+==Crystal structure of VosA-VelB-complex==
+<StructureSection load='4n6r' size='340' side='right'caption='[[4n6r]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4n6r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_nidulans Aspergillus nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N6R FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4n6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n6r OCA], [https://pdbe.org/4n6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n6r RCSB], [https://www.ebi.ac.uk/pdbsum/4n6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n6r ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/VOSA_EMENI VOSA_EMENI] Component of the velB-VosA heterodimeric complex that plays a dual role in activating genes associated with spore maturation and repressing certain development-associated genes (PubMed:17912349, PubMed:21152013, PubMed:23049895, PubMed:24391470). Controls primarily the late process of sporulation including trehalose biogenesis (PubMed:17912349). The complex binds DNA through the DNA-binding domain of vosA that recognizes an 11-nucleotide consensus sequence 5'-CTGGCCGCGGC-3' consisting of two motifs in the promoters of key developmental regulatory genes (PubMed:24391470). The vosA-velB complex binds to the beta-glucan synthase fksA gene promoter in asexual spores for repression (PubMed:25960370).[UniProtKB:A0SP16]<ref>PMID:17912349</ref> <ref>PMID:21152013</ref> <ref>PMID:23049895</ref> <ref>PMID:25960370</ref>
+<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.
-Authors: Ahmend, Y.L., Dickmanns, A., Neumann, P., Ficner, R.
+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>
-Description: Crystal structure of VosA-VelB-complex
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4n6r" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Aspergillus nidulans]]
+[[Category: Large Structures]]
+[[Category: Ahmed YL]]
+[[Category: Dickmanns A]]
+[[Category: Ficner R]]
+[[Category: Neumann P]]

4n6r

From Proteopedia

Current revision

Crystal structure of VosA-VelB-complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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