ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structure of bacterial LigD 3'-phosphoesterase unveils a DNA repair superfamily.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- Oligomerisation of Ku from Mycobacterium tuberculosis promotes DNA synapsis.Nature communications · 2025Article
- Conservation and divergence of ciprofloxacin persister survival mechanisms between Pseudomonas aeruginosa and Escherichia coli.PLoS genetics · 2025Article
- Nucleic acid joining enzymes: biological functions and synthetic applications beyond DNA.The Biochemical journal · 2025Review
- Structural Bioinformatics and Deep Learning of Metalloproteins: Recent Advances and Applications.International journal of molecular sciences · 2022Review
- LigD: A Structural Guide to the Multi-Tool of Bacterial Non-Homologous End Joining.Frontiers in molecular biosciences · 2021Review
- Structural insight into DNA joining: from conserved mechanisms to diverse scaffolds.Nucleic acids research · 2020Review
- 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
- Article
- Biochemical and Structural Characterisation of DNA Ligases from Bacteria and Archaea.Bioscience reports · 2016Article
- Molecular basis for DNA strand displacement by NHEJ repair polymerases.Nucleic acids research · 2016Article
- DNA ligase C1 mediates the LigD-independent nonhomologous end-joining pathway of Mycobacterium smegmatis.Journal of bacteriology · 2014Article
- Impact of DNA3'pp5'G capping on repair reactions at DNA 3' ends.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Rewriting the rules for end joining via enzymatic splicing of DNA 3'-PO4 and 5'-OH ends.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Discrimination of RNA from DNA by polynucleotide phosphorylase.Biochemistry · 2013Article
- Ribonucleolytic resection is required for repair of strand displaced nonhomologous end-joining intermediates.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Distinctive effects of domain deletions on the manganese-dependent DNA polymerase and DNA phosphorylase activities of Mycobacterium smegmatis polynucleotide phosphorylase.Biochemistry · 2013Article
- Characterization of Mycobacterium smegmatis PolD2 and PolD1 as RNA/DNA polymerases homologous to the POL domain of bacterial DNA ligase D.Biochemistry · 2012Article
- Solution structure and DNA-binding properties of the phosphoesterase domain of DNA ligase D.Nucleic acids research · 2012Article
- Structural insights to the metal specificity of an archaeal member of the LigD 3'-phosphoesterase DNA repair enzyme family.Nucleic acids research · 2012Article
- Sequence-specific 1H, 13C and 15N assignments of the phosphoesterase (PE) domain of Pseudomonas aeruginosa DNA ligase D (LigD).Biomolecular NMR assignments · 2011Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The DNA ligase D (LigD) 3'-phosphoesterase (PE) module is a conserved component of the bacterial nonhomologous end-joining (NHEJ) apparatus that performs 3' end-healing reactions at DNA double-strand breaks. Here we report the 1.9 A crystal structure of Pseudomonas aeruginosa PE, which reveals that PE exemplifies a unique class of DNA repair enzyme. PE has a distinctive fold in which an eight stranded beta barrel with a hydrophobic interior supports a crescent-shaped hydrophilic active site on its outer surface. Six essential side chains coordinate manganese and a sulfate mimetic of the scissile phosphate. The PE active site and mechanism are unique vis à vis other end-healing enzymes. We find PE homologs in archaeal and eukaryal proteomes, signifying that PEs comprise a DNA repair superfamily.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.