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Sequence-specific 1HN, 13C, and 15N backbone resonance assignments of the 34 kDa Paramecium bursaria Chlorella virus 1 (PBCV1) DNA ligase
- Source :
- Biomolecular NMR Assignments. 3:77-80
- Publication Year :
- 2009
- Publisher :
- Springer Science and Business Media LLC, 2009.
-
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 beta-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.
- Subjects :
- Magnetic Resonance Spectroscopy
Paramecium
DNA Ligases
Molecular Sequence Data
Biochemistry
Article
Viral Proteins
chemistry.chemical_compound
Structural Biology
Animals
A-DNA
Amino Acid Sequence
Peptide sequence
chemistry.chemical_classification
Carbon Isotopes
DNA ligase
Nitrogen Isotopes
biology
Nuclear magnetic resonance spectroscopy
Nucleotidyltransferase
biology.organism_classification
Molecular Weight
chemistry
Protons
DNA
Subjects
Details
- ISSN :
- 1874270X and 18742718
- Volume :
- 3
- Database :
- OpenAIRE
- Journal :
- Biomolecular NMR Assignments
- Accession number :
- edsair.doi.dedup.....41a8846baf3b71cc58b4dcc46e6d5c5e