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

   

Authors:	Dutta, K.; Natarajan, A.; Nair, P. A.; Shuman, S.; Ghose, R.
Article Title:	Sequence-specific (1)H, (13)C and (15)N 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.
Keywords:	dna repair; protein; repair; dna ligase; non-homologous end-joining; bacterial
Journal Title:	Biomolecular NMR Assignments
Volume:	5
Issue:	2
ISSN:	1874-2718
Publisher:	Springer
Date Published:	2011-10-01
Start Page:	151
End Page:	155
Language:	English
DOI:	10.1007/s12104-010-9289-7
ACCESSION:	WOS:000294559700007
PROVIDER:	wos
PUBMED:	21213076
PMCID:	PMC4156853
Notes:	--- - Article - "Source: Wos"

https://synapse.mskcc.org/synapse/works/has_related_data_chk/13675