4N6Q
Crystal structure of VosA velvet domain
Summary for 4N6Q
| Entry DOI | 10.2210/pdb4n6q/pdb |
| Related | 4N6R |
| Descriptor | VosA, IODIDE ION, NITRATE ION, ... (4 entities in total) |
| Functional Keywords | ig-fold, nfkb, beta-sandwich, transcription factor, velb, dna binding protein |
| Biological source | Emericella nidulans |
| Total number of polymer chains | 1 |
| Total formula weight | 23096.31 |
| Authors | Ahmed, Y.L.,Dickmanns, A.,Neumann, P.,Ficner, R. (deposition date: 2013-10-14, release date: 2014-01-22, Last modification date: 2024-02-28) |
| Primary citation | Ahmed, Y.L.,Gerke, J.,Park, H.S.,Bayram, O.,Neumann, P.,Ni, M.,Dickmanns, A.,Kim, S.C.,Yu, J.H.,Braus, G.H.,Ficner, R. The Velvet Family of Fungal Regulators Contains a DNA-Binding Domain Structurally Similar to NF-kappa B. Plos Biol., 11:e1001750-e1001750, 2013 Cited by PubMed Abstract: 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-κB. 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. PubMed: 24391470DOI: 10.1371/journal.pbio.1001750 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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