Sequence-specific backbone ¹H, ¹³C and ¹⁵N assignments of the catalytic domain of the Escherichia coli protein tyrosine kinase, Wzc

Biomol NMR Assign. 2014 Apr;8(1):37-41. doi: 10.1007/s12104-012-9448-0. Epub 2012 Dec 8.


Protein tyrosine kinases in bacteria are structurally and functionally distinct from their eukaryotic counterparts. The largest family of bacterial tyrosine kinases, the BY-kinase family, is highly conserved in Gram-negative and Gram-positive species, and plays a central role in biofilm and capsule formation. In Escherichia coli the BY-kinase, Wzc, is a critical component of the machinery responsible for the synthesis and export of the exo-polysaccharide colanic acid, a key constituent of biofilms. Here we present the main-chain (1)H(N), (15)N, (13)C' and (13)Cα, side-chain (13)Cβ resonance assignments for a construct that encodes the entire 274-residue cytosolic catalytic domain of Wzc.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Carbon Isotopes
  • Catalytic Domain*
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins / chemistry*
  • Hydrogen
  • Membrane Proteins / chemistry*
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Structure, Secondary
  • Protein-Tyrosine Kinases / chemistry*


  • Carbon Isotopes
  • Escherichia coli Proteins
  • Membrane Proteins
  • Nitrogen Isotopes
  • Hydrogen
  • Protein-Tyrosine Kinases
  • wzc protein, E coli