4N6Q

Crystal structure of VosA velvet domain

4N6Q の概要

• エントリーDOI: 10.2210/pdb4n6q/pdb
• 関連するPDBエントリー: 4N6R
• 分子名称: VosA, IODIDE ION, NITRATE ION, ... (4 entities in total)
• 機能のキーワード: ig-fold, nfkb, beta-sandwich, transcription factor, velb, dna binding protein
• 由来する生物種: Emericella nidulans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23096.31

構造登録者

Ahmed, Y.L.,Dickmanns, A.,Neumann, P.,Ficner, R. (登録日: 2013-10-14, 公開日: 2014-01-22, 最終更新日: 2024-02-28)

主引用文献

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

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: 24391470
DOI: 10.1371/journal.pbio.1001750

実験手法

X-RAY DIFFRACTION (1.79 Å)