title: 1H, 13C, and 15N NMR assignments of the Pyrococcus abyssi DNA polymerase II intein.
abstract: Protein splicing is a precise post-translational process mediated by inteins. Inteins are intervening proteins that cleave themselves from a precursor protein while joining the flanking sequences. Here we report the (15)N, (13)C, and (1)H chemical shift assignments of the intein from DNA polymerase II of Pyrococcus abyssi (Pab PolII intein), which has been recombinantly overexpressed and isotopically labeled. The NMR assignments of Pab PolII intein are essential for solution structure determination and protein dynamics study.
authors.affiliation: Biology Department, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
authors.forename: Jiajing
authors.initials: J
authors.lastname: Liu
authors.forename: Zhenming
authors.initials: Z
authors.lastname: Du
authors.forename: Clayton D
authors.initials: CD
authors.lastname: Albracht
authors.forename: Roshni O
authors.initials: RO
authors.lastname: Naidu
authors.forename: Kenneth V
authors.initials: KV
authors.lastname: Mills
authors.forename: Chunyu
authors.initials: C
authors.lastname: Wang
mesh_terms: D004257:DNA Polymerase II / Q000737:chemistry*; D047668:Inteins; D007554:Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D043903:Pyrococcus abyssi / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D007554:Isotopes; D011994:Recombinant Proteins; D004257:DNA Polymerase II