ArticleNucleic acids research2018
DNA binding with a minimal scaffold: structure-function analysis of Lig E DNA ligases.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Cloning and Functional Characterization of AhyAP-T65Lig, an ATP-Dependent DNA Ligase from Trabzonvirus AP-T65.Molecular biotechnology · 2026Article
- Crystal structure of ATP-dependent DNA ligase from Rhizobium phage vB_RleM_P10VF.Acta crystallographica. Section F, Structural biology communications · 2025Article
- A role for the ATP-dependent DNA ligase lig E of Neisseria gonorrhoeae in biofilm formation.BMC microbiology · 2024Article
- Horizontal acquisition of a DNA ligase improves DNA damage tolerance in eukaryotes.Nature communications · 2023Article
- Bacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase.Scientific reports · 2021Article
- Structural insight into DNA joining: from conserved mechanisms to diverse scaffolds.Nucleic acids research · 2020Review
- Structural intermediates of a DNA-ligase complex illuminate the role of the catalytic metal ion and mechanism of phosphodiester bond formation.Nucleic acids research · 2019Article
- Rational design of an XNA ligase through docking of unbound nucleic acids to toroidal proteins.Nucleic acids research · 2019Article
- Temperature adaptation of DNA ligases from psychrophilic organisms.Extremophiles : life under extreme conditions · 2019Article
- Structures of ATP-bound DNA ligase D in a closed domain conformation reveal a network of amino acid and metal contacts to the ATP phosphates.The Journal of biological chemistry · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA ligases join breaks in the phosphodiester backbone of DNA by catalysing the formation of bonds between opposing 5'P and 3'OH ends in an adenylation-dependent manner. Catalysis is accompanied by reorientation of two core domains to provide access to the active site for cofactor utilization and enable substrate binding and product release. The general paradigm is that DNA ligases engage their DNA substrate through complete encirclement of the duplex, completed by inter-domain kissing contacts via loops or additional domains. The recent structure of a minimal Lig E-type DNA ligase, however, implies it must use a different mechanism, as it lacks any domains or loops appending the catalytic core which could complete encirclement. In the present study, we have used a structure-guided mutagenesis approach to investigate the role of conserved regions in the Lig E proteins with respect to DNA binding. We report the structure of a Lig-E type DNA ligase bound to the nicked DNA-adenylate reaction intermediate, confirming that complete encirclement is unnecessary for substrate engagement. Biochemical and biophysical measurements of point mutants to residues implicated in binding highlight the importance of basic residues in the OB domain, and inter-domain contacts to the linker.
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