8R7Y
Deoxyribonucleoside regulator DeoR in complex with the DNA operator
8R7Y の概要
| エントリーDOI | 10.2210/pdb8r7y/pdb |
| 分子名称 | Deoxyribonucleoside regulator, OL18 DNA operator, strand 1, OL18 DNA operator, strand 2, ... (4 entities in total) |
| 機能のキーワード | transcriptional repressor, protein-dna complex, bacillus subtilis, dna binding protein |
| 由来する生物種 | Bacillus subtilis subsp. subtilis str. 168 詳細 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 165239.19 |
| 構造登録者 | |
| 主引用文献 | Soltysova, M.,Skerlova, J.,Pachl, P.,Skubnik, K.,Fabry, M.,Sieglova, I.,Farolfi, M.,Grishkovskaya, I.,Babiak, M.,Novacek, J.,Krasny, L.,Rezacova, P. Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function. Nucleic Acids Res., 52:7305-7320, 2024 Cited by PubMed Abstract: The SorC family of transcriptional regulators plays a crucial role in controlling the carbohydrate metabolism and quorum sensing. We employed an integrative approach combining X-ray crystallography and cryo-electron microscopy to investigate architecture and functional mechanism of two prototypical representatives of two sub-classes of the SorC family: DeoR and CggR from Bacillus subtilis. Despite possessing distinct DNA-binding domains, both proteins form similar tetrameric assemblies when bound to their respective DNA operators. Structural analysis elucidates the process by which the CggR-regulated gapA operon is derepressed through the action of two effectors: fructose-1,6-bisphosphate and newly confirmed dihydroxyacetone phosphate. Our findings provide the first comprehensive understanding of the DNA binding mechanism of the SorC-family proteins, shedding new light on their functional characteristics. PubMed: 38842936DOI: 10.1093/nar/gkae434 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.7 Å) |
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