| Literature DB >> 21213076 |
Kaushik Dutta1, Aswin Natarajan, Pravin A Nair, Stewart Shuman, Ranajeet Ghose.
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.Entities:
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Year: 2011 PMID: 21213076 PMCID: PMC4156853 DOI: 10.1007/s12104-010-9289-7
Source DB: PubMed Journal: Biomol NMR Assign ISSN: 1874-270X Impact factor: 0.746