Sequence-specific 1H, 13C and 15N assignments of the phosphoesterase (PE) domain of Pseudomonas aeruginosa DNA ligase D (LigD)

Biomol NMR Assign. 2011 Oct;5(2):151-5. doi: 10.1007/s12104-010-9289-7. Epub 2011 Jan 7.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Carbon Isotopes
  • DNA Ligases / chemistry*
  • DNA Repair
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular*
  • Phosphoric Monoester Hydrolases / chemistry*
  • Protein Structure, Tertiary
  • Pseudomonas aeruginosa / chemistry
  • Pseudomonas aeruginosa / enzymology*


  • Bacterial Proteins
  • Carbon Isotopes
  • Nitrogen Isotopes
  • Phosphoric Monoester Hydrolases
  • DNA Ligases