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Sequence-specific 1H, 13C and 15N assignments of the phosphoesterase (PE) domain of Pseudomonas aeruginosa DNA ligase D (LigD)
- Source :
- Biomolecular NMR Assignments. 5:151-155
- Publication Year :
- 2011
- Publisher :
- Springer Science and Business Media LLC, 2011.
-
Abstract
- DNA ligase D (LigD), consisting of polymerase, ligase and phosphoesterase domains, is the essential catalyst of the bacterial non-homologous end-joining pathway of DNA double-strand break repair. The phosphoesterase (PE) module performs manganese-dependent 3'-phosphomonoesterase and 3'-ribonucleoside resection reactions that heal broken ends in preparation for sealing. LigD PE exemplifies a structurally and mechanistically unique class of DNA end-processing enzymes. Here, we present the resonance assignments of the PE domain of Pseudomonas aeruginosa LigD comprising the N-terminal 177 residues.
- Subjects :
- DNA Ligases
DNA Repair
DNA repair
medicine.disease_cause
Biochemistry
Article
chemistry.chemical_compound
Bacterial Proteins
Structural Biology
medicine
Nuclear Magnetic Resonance, Biomolecular
Polymerase
chemistry.chemical_classification
Carbon Isotopes
DNA ligase
Nitrogen Isotopes
biology
Pseudomonas aeruginosa
Phosphoric Monoester Hydrolases
Protein Structure, Tertiary
Non-homologous end joining
Enzyme
chemistry
biology.protein
DNA
Subjects
Details
- ISSN :
- 1874270X and 18742718
- Volume :
- 5
- Database :
- OpenAIRE
- Journal :
- Biomolecular NMR Assignments
- Accession number :
- edsair.doi.dedup.....4e8eef510fae5adf338b01b594808c50