Abstract：
:YbeA is a 3-methylpseudoridine methyltransferase from Escherichia coli that forms a stable homodimer in solution. It is one of the deeply trefoil 31 knotted proteins, of which the knot encompasses the C-terminal helix that threads through a long loop. Recent studies on the knotted protein folding pathways using YbeA have suggested that the protein knot remains present under chemically denaturing conditions. Here, we report (1)H, (13)C and (15)N chemical shift assignments for urea-denatured YbeA, which will serve as the basis for further structural characterisations using solution state NMR spectroscopy with paramagnetic spin labeled and partial alignment media.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Hsieh SJ,Mallam AL,Jackson SE,Hsu STdoi
10.1007/s12104-013-9501-7subject
Has Abstractpub_date
2014-10-01 00:00:00pages
283-5issue
2eissn
1874-2718issn
1874-270Xjournal_volume
8pub_type
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