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.
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Acknowledgments
This work was supported by the following grants: NSF MCB 083141 (RG); NIH GM63611 (SS) and NIH 5G12 RR03060 (partial support of the core facilities at CCNY). SS is an American Cancer Society Research Professor. RG is a member of the New York Structural Biology Center, a STAR center supported by the New York State Office for Science, Technology and Academic Research.
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Kaushik Dutta and Aswin Natarajan contributed equally to this work.
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Dutta, K., Natarajan, A., Nair, P.A. et al. Sequence-specific 1H, 13C and 15N assignments of the phosphoesterase (PE) domain of Pseudomonas aeruginosa DNA ligase D (LigD). Biomol NMR Assign 5, 151–155 (2011). https://doi.org/10.1007/s12104-010-9289-7
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DOI: https://doi.org/10.1007/s12104-010-9289-7