6ON0

STRUCTURE OF N15 CRO COMPLEXED WITH CONSENSUS OPERATOR DNA

「3QWS」から置き換えられました

6ON0 の概要

• エントリーDOI: 10.2210/pdb6on0/pdb
• 関連するPDBエントリー: 2HIN
• 分子名称: Gp39, DNA (5'-D(*TP*TP*TP*AP*TP*AP*GP*CP*TP*AP*GP*CP*TP*AP*TP*AP*A)-3') (3 entities in total)
• 機能のキーワード: transcription repressor-dna complex, helix-turn-helix, lambda repressor-like dna-binding domain, structural evolution, transcription-dna complex, transcription/dna
• 由来する生物種: Escherichia phage N15; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 26080.57

構造登録者

Hall, B.M.,Roberts, S.A.,Cordes, M.H.J. (登録日: 2019-04-19, 公開日: 2019-05-15, 最終更新日: 2023-10-11)

主引用文献

Hall, B.M.,Roberts, S.A.,Cordes, M.H.J.
Extreme divergence between one-to-one orthologs: the structure of N15 Cro bound to operator DNA and its relationship to the lambda Cro complex.
Nucleic Acids Res., 47:7118-7129, 2019

PubMed Abstract: The gene cro promotes lytic growth of phages through binding of Cro protein dimers to regulatory DNA sites. Most Cro proteins are one-to-one orthologs, yet their sequence, structure and binding site sequences are quite divergent across lambdoid phages. We report the cocrystal structure of bacteriophage N15 Cro with a symmetric consensus site. We contrast this complex with an orthologous structure from phage λ, which has a dissimilar binding site sequence and a Cro protein that is highly divergent in sequence, dimerization interface and protein fold. The N15 Cro complex has less DNA bending and smaller DNA-induced changes in protein structure. N15 Cro makes fewer direct contacts and hydrogen bonds to bases, relying mostly on water-mediated and Van der Waals contacts to recognize the sequence. The recognition helices of N15 Cro and λ Cro make mostly nonhomologous and nonanalogous contacts. Interface alignment scores show that half-site binding geometries of N15 Cro and λ Cro are less similar to each other than to distantly related CI repressors. Despite this divergence, the Cro family shows several code-like protein-DNA sequence covariations. In some cases, orthologous genes can achieve a similar biological function using very different specific molecular interactions.

PubMed: 31180482
DOI: 10.1093/nar/gkz507

実験手法

X-RAY DIFFRACTION (1.6 Å)