Sequence-specific (1)H(N), (13)C, and (15)N backbone resonance assignments of the 34 kDa Paramecium bursaria Chlorella virus 1 (PBCV1) DNA ligase Journal Article
| Authors: | Piserchio, A.; Nair, P. A.; Shuman, S.; Ghose, R. |
| Article Title: | Sequence-specific (1)H(N), (13)C, and (15)N backbone resonance assignments of the 34 kDa Paramecium bursaria Chlorella virus 1 (PBCV1) DNA ligase |
| Abstract: | Chlorella virus DNA ligase (ChVLig) is a minimal (298-amino acid) pluripotent ATP-dependent ligase composed of three structural modules-a nucleotidyltransferase domain, an OB domain, and a β-hairpin latch-that forms a circumferential clamp around nicked DNA. ChVLig provides an instructive model to understand the chemical and conformational steps of nick repair. Here we report the assignment of backbone (13)C, (15)N, (1)H(N) resonances of this 34.2 kDa protein, the first for a DNA ligase in full-length form. © 2009 Springer Science+Business Media B.V. |
| Keywords: | molecular genetics; methodology; animal; animals; virology; chemistry; amino acid sequence; molecular sequence data; magnetic resonance spectroscopy; nuclear magnetic resonance spectroscopy; protons; dna binding; polydeoxyribonucleotide synthase; molecular weight; nitrogen; chlorella virus; dna ligase; dna nick repair; paramecium; paramecium bursaria chlorella virus 1; carbon; chlorella virus dna ligase; proton; virus protein; carbon isotopes; dna ligases; nitrogen isotopes; viral proteins |
| Journal Title: | Biomolecular NMR Assignments |
| Volume: | 3 |
| Issue: | 1 |
| ISSN: | 1874-2718 |
| Publisher: | Springer |
| Date Published: | 2009-06-01 |
| Start Page: | 77 |
| End Page: | 80 |
| Language: | English |
| DOI: | 10.1007/s12104-009-9145-9 |
| PUBMED: | 19636951 |
| PROVIDER: | scopus |
| PMCID: | PMC2746884 |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 1" - "Export Date: 30 November 2010" - "Source: Scopus" |
Altmetric
Citation Impact
BMJ Impact Analytics
Related MSK Work