Sequence-specific 1HN, 13C, and 15N backbone resonance assignments of the 34 kDa Paramecium bursaria Chlorella virus 1 (PBCV1) DNA ligase

descriptionPublicationkeyboard_double_arrow_right Article 13 Jan 2009 English Publisher:Springer Science and Business Media LLCJournal:Biomolecular NMR Assignments, volume 3, pages 77-80 (issn: 1874-2718, eissn: 1874-270X,

Copyright policy )Funded by:NSF | Acquisition of a 600 MHz ..., NIH | SEQ OF DNA CONTAINING SV4..., NIH | 900 MHz NMR Spectrometer ... +1 projects

Authors: Andrea, Piserchio; Pravin A, Nair; Stewart, Shuman; Ranajeet, Ghose;

doi: 10.1007/s12104-009-9145-9

pmid: 19636951

pmc: PMC2746884

Sequence-specific 1HN, 13C, and 15N backbone resonance assignments of the 34 kDa Paramecium bursaria Chlorella virus 1 (PBCV1) DNA ligase

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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.

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Keywords

Carbon Isotopes, Magnetic Resonance Spectroscopy, Paramecium, DNA Ligases, Nitrogen Isotopes, Molecular Sequence Data, Molecular Weight, Viral Proteins, Animals, Amino Acid Sequence, Protons

2 Research products, page 1 of 1

Kinetic Analysis of DNA Strand Joining by Chlorella Virus DNA Ligase and the Role of Nucleotidyltransferase Motif VI in Ligase Adenylylation
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