Backbone NMR assignments of a topologically knotted protein in urea-denatured state

YibK is a tRNA methyltransferase from Haemophilus influenzae , which forms a stable homodimer in solution and contains a deep trefoil 3 1 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 dat...

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Bibliographic Details
Published in:Biomolecular NMR assignments 2014-10, Vol.8 (2), p.439-442
Main Authors: Hsieh, Shu-Ju Micky, Mallam, Anna L., Jackson, Sophie E., Hsu, Shang-Te Danny
Format: Article
Language:English
Subjects:
Biochemistry
Biological and Medical Physics
Biophysics
NMR
Nuclear magnetic resonance
Physics
Physics and Astronomy
Polymer Sciences
Protein folding
Proteins
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Summary:YibK is a tRNA methyltransferase from Haemophilus influenzae , which forms a stable homodimer in solution and contains a deep trefoil 3 1 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.
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-013-9510-6