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

Authors :
Aswin Natarajan
Ranajeet Ghose
Kaushik Dutta
Pravin A. Nair
Stewart Shuman
Source :
Biomolecular NMR Assignments. 5:151-155
Publication Year :
2011
Publisher :
Springer Science and Business Media LLC, 2011.

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.

Details

ISSN :
1874270X and 18742718
Volume :
5
Database :
OpenAIRE
Journal :
Biomolecular NMR Assignments
Accession number :
edsair.doi.dedup.....4e8eef510fae5adf338b01b594808c50