6on0 | pdb_00006on0
STRUCTURE OF N15 CRO COMPLEXED WITH CONSENSUS OPERATOR DNA
Structural highlights
FunctionPublication Abstract from PubMedThe 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 lambda, 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 lambda Cro make mostly nonhomologous and nonanalogous contacts. Interface alignment scores show that half-site binding geometries of N15 Cro and lambda 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. Extreme divergence between one-to-one orthologs: the structure of N15 Cro bound to operator DNA and its relationship to the lambda Cro complex.,Hall BM, Roberts SA, Cordes MHJ Nucleic Acids Res. 2019 Jun 10. pii: 5513319. doi: 10.1093/nar/gkz507. PMID:31180482[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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