The high-precision solution structure of Yersinia modulating protein YmoA provides insight into interaction with H-NS

Biochemistry. 2007 Dec 11;46(49):13975-82. doi: 10.1021/bi701210j. Epub 2007 Nov 15.


The high-resolution solution structure of Yersinia modulating protein YmoA is presented. The protein is all helical with the first three of four helices forming the central core. Structures calculated with only NOE and dihedral restraints exhibit a backbone root-mean-square deviation (rmsd) of 0.77 A. Upon refinement against Halpha-Calpha, HN-N, and Calpha-C' J-modulated residual dipolar couplings, the backbone rmsd improves to 0.22 A. YmoA has a high amino acid sequence identity to and a similar overall fold to Escherichia coli hemolysin expression modulating protein Hha; however, structural differences do occur. YmoA is also found to be structurally similar to the histone-like nucleoid structuring protein H-NS, indicating that YmoA may intercalate into higher-order H-NS suprastructuring by substituting for an H-NS dimer.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • DNA-Binding Proteins / chemistry*
  • Escherichia coli Proteins / chemistry
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Sequence Alignment
  • Yersinia enterocolitica / chemistry


  • Bacterial Proteins
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • H-NS protein, bacteria
  • YmoA protein, Yersinia enterocolitica
  • hha protein, E coli

Associated data

  • PDB/2JVP