ArticleNucleic acids research2011
Asymmetric DNA recognition by the OkrAI endonuclease, an isoschizomer of BamHI.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Noncanonical DNA Cleavage by BamHI Endonuclease in Laterally Confined DNA Monolayers Is a Step Function of DNA Density and Sequence.Molecules (Basel, Switzerland) · 2022Article
- Probing DNA-protein interactions using single-molecule diffusivity contrast.Biophysical reports · 2021Article
- Mismodeled purines: implicit alternates and hidden Hoogsteens.Acta crystallographica. Section D, Structural biology · 2017Article
- Increasing cleavage specificity and activity of restriction endonuclease KpnI.Nucleic acids research · 2013Article
- Catalytic domain of plasmid pAD1 relaxase TraX defines a group of relaxases related to restriction endonucleases.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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7 authors.
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Abstract
Restriction enzymes share little or no sequence homology with the exception of isoschizomers, or enzymes that recognize and cleave the same DNA sequence. We present here the structure of a BamHI isoschizomer, OkrAI, bound to the same DNA sequence (TATGGATCCATA) as that cocrystallized with BamHI. We show that OkrAI is a more minimal version of BamHI, lacking not only the N- and C-terminal helices but also an internal 3(10) helix and containing β-strands that are shorter than those in BamHI. Despite these structural differences, OkrAI recognizes the DNA in a remarkably similar manner to BamHI, including asymmetric contacts via C-terminal 'arms' that appear to 'compete' for the minor groove. However, the arms are shorter than in BamHI. We observe similar DNA-binding affinities between OkrAI and BamHI but OkrAI has higher star activity (at 37°C) compared to BamHI. Together, the OkrAI and BamHI structures offer a rare opportunity to compare two restriction enzymes that work on exactly the same DNA substrate.
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