Summary for 6ON0
| Entry DOI | 10.2210/pdb6on0/pdb | 
| Related | 2HIN | 
| Descriptor | 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) | 
| Functional Keywords | transcription repressor-dna complex, helix-turn-helix, lambda repressor-like dna-binding domain, structural evolution, transcription-dna complex, transcription/dna | 
| Biological source | Escherichia phage N15 More  | 
| Total number of polymer chains | 4 | 
| Total formula weight | 26080.57 | 
| Authors | Hall, B.M.,Roberts, S.A.,Cordes, M.H.J. (deposition date: 2019-04-19, release date: 2019-05-15, Last modification date: 2023-10-11)  | 
| Primary citation | 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 Cited by  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: 31180482DOI: 10.1093/nar/gkz507 PDB entries with the same primary citation  | 
| Experimental method | X-RAY DIFFRACTION (1.6 Å)  | 
Structure validation
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