title: Backbone 1H, 13C and 15N assignments of YibK and avariant containing a unique cysteine residue at C-terminus in 8 M urea-denatured states [corrected].
abstract: YibK is a tRNA methyltransferase from Haemophilus influenzae, which forms a stable homodimer in solution and contains a deep trefoil 31 knot encompassing the C-terminal helix that threads through a long loop. It has been a model system for investigating knotted protein folding pathways. Recent data have shown that the polypeptide chain of YibK remains loosely knotted under highly denaturing conditions. Here, we report (1)H, (13)C and (15)N chemical shift assignments for YibK and its variant in the presence of 8 M urea. This work forms the basis for further analysis using NMR techniques such as paramagnetic relaxation enhancement, residual dipolar couplings and spin-relaxation dynamics analysis.
authors.affiliation: Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
authors.forename: Shu-Ju Micky
authors.initials: SJ
authors.lastname: Hsieh
authors.forename: Anna L
authors.initials: AL
authors.lastname: Mallam
authors.forename: Sophie E
authors.initials: SE
authors.lastname: Jackson
authors.forename: Shang-Te Danny
authors.initials: ST
authors.lastname: Hsu
mesh_terms: D006193:Haemophilus influenzae / Q000201:enzymology; D008780:Methyltransferases / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011489:Protein Denaturation / Q000187:drug effects*; D013113:Spin Labels; D014508:Urea / Q000494:pharmacology*
chemical_list: D013113:Spin Labels; D014508:Urea; D008780:Methyltransferases