title: Sequence-specific 1H N, 13C, and 15N 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 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.
authors.affiliation: Department of Chemistry, The City College of New York, 160 Convent Avenue, New York, NY 10031, USA.
authors.forename: Andrea
authors.initials: A
authors.lastname: Piserchio
authors.forename: Pravin A
authors.initials: PA
authors.lastname: Nair
authors.forename: Stewart
authors.initials: S
authors.lastname: Shuman
authors.forename: Ranajeet
authors.initials: R
authors.lastname: Ghose
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002247:Carbon Isotopes / Q000737:chemistry; D011088:DNA Ligases / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D010247:Paramecium / Q000821:virology*; D011522:Protons; D014764:Viral Proteins / Q000737:chemistry*
chemical_list: D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; D014764:Viral Proteins; C110456:Chlorella virus DNA ligase; D011088:DNA Ligases