ArticleNucleic acids research2013
The structure of Escherichia coli ExoIX--implications for DNA binding and catalysis in flap endonucleases.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 19 citations in OpenAlex.
- Single-molecule tracking of RNA-DNA hybrid removal enzymes important for lagging-strand replication.Biophysical journal · 2026Article
- DNA polymerase I: structure, activity, and function in bacterial DNA replication and repair.Critical reviews in biochemistry and molecular biology · 2026Review
- Single-molecule tracking of RNA-DNA hybrid removal enzymes important for lagging-strand replication.bioRxiv : the preprint server for biology · 2025Article
- Article
- R-loop control and mitochondrial genome stability require the 5'-3' exonuclease/flap endonuclease OEX1.The Plant cell · 2025Article
- Article
- Bacillus subtilis encodes a discrete flap endonuclease that cleaves RNA-DNA hybrids.PLoS genetics · 2023Article
- Crystal structure and mutational analysis of Mycobacterium smegmatis FenA highlight active site amino acids and three metal ions essential for flap endonuclease and 5' exonuclease activities.Nucleic acids research · 2018Article
- The DNA Repair Repertoire of Mycobacterium smegmatis FenA Includes the Incision of DNA 5' Flaps and the Removal of 5' Adenylylated Products of Aborted Nick Ligation.Journal of bacteriology · 2017Article
- Comprehensive classification of the PIN domain-like superfamily.Nucleic acids research · 2017Article
- Direct observation of DNA threading in flap endonuclease complexes.Nature structural & molecular biology · 2016Article
- Crystal structure of the catalytic core of Rad2: insights into the mechanism of substrate binding.Nucleic acids research · 2014Article
- Molecular insights into the prototypical single-stranded DNA-binding protein fromCritical reviews in biochemistry and molecular biologyReview
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Escherichia coli Exonuclease IX (ExoIX), encoded by the xni gene, was the first identified member of a novel subfamily of ubiquitous flap endonucleases (FENs), which possess only one of the two catalytic metal-binding sites characteristic of other FENs. We have solved the first structure of one of these enzymes, that of ExoIX itself, at high resolution in DNA-bound and DNA-free forms. In the enzyme-DNA cocrystal, the single catalytic site binds two magnesium ions. The structures also reveal a binding site in the C-terminal domain where a potassium ion is directly coordinated by five main chain carbonyl groups, and we show this site is essential for DNA binding. This site resembles structurally and functionally the potassium sites in the human FEN1 and exonuclease 1 enzymes. Fluorescence anisotropy measurements and the crystal structures of the ExoIX:DNA complexes show that this potassium ion interacts directly with a phosphate diester in the substrate DNA.
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