Unknown

Dataset Information

0

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.

SUBMITTER: Dutta K 

PROVIDER: S-EPMC4156853 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Dutta Kaushik K   Natarajan Aswin A   Nair Pravin A PA   Shuman Stewart S   Ghose Ranajeet R  

Biomolecular NMR assignments 20110107 2


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 resonanc  ...[more]

Similar Datasets

| S-EPMC3049224 | biostudies-literature
| S-EPMC5944331 | biostudies-literature
| S-EPMC6439258 | biostudies-literature
| S-EPMC2862173 | biostudies-literature
| S-EPMC3438405 | biostudies-literature
| S-EPMC7091140 | biostudies-literature
| S-EPMC2947601 | biostudies-literature
| S-EPMC6439154 | biostudies-literature