title: Sequence-specific 1H, 13C and 15N assignments of the phosphoesterase (PE) domain of Pseudomonas aeruginosa DNA ligase D (LigD).
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.
authors.affiliation: The New York Structural Biology Center, 89 Convent Avenue, New York, NY 10027, USA.
authors.forename: Kaushik
authors.initials: K
authors.lastname: Dutta
authors.forename: Aswin
authors.initials: A
authors.lastname: Natarajan
authors.forename: Pravin A
authors.initials: PA
authors.lastname: Nair
authors.forename: Stewart
authors.initials: S
authors.lastname: Shuman
authors.forename: Ranajeet
authors.initials: R
authors.lastname: Ghose
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D011088:DNA Ligases / Q000737:chemistry*; D004260:DNA Repair; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D011550:Pseudomonas aeruginosa / Q000737:chemistry / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D010744:Phosphoric Monoester Hydrolases; D011088:DNA Ligases