Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins

FEBS Lett. 2005 Oct 24;579(25):5669-74. doi: 10.1016/j.febslet.2005.09.045. Epub 2005 Oct 4.


New relationships found in the process of updating the structural classification of proteins (SCOP) database resulted in the revision of the structure of the N-terminal, DNA-binding domain of the transition state regulator AbrB. The dimeric AbrB domain shares a common fold with the addiction antidote MazE and the subunit of uncharacterized protein MraZ implicated in cell division and cell envelope formation. It has a detectable sequence similarity to both MazE and MraZ thus providing an evolutionary link between the two proteins. The putative DNA-binding site of AbrB is found on the same face as the DNA-binding site of MazE and appears similar, both in structure and sequence, to the exposed conserved region of MraZ. This strongly suggests that MraZ also binds DNA and allows for a consensus model of DNA recognition by the members of this novel protein superfamily.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / metabolism
  • Bacterial Proteins
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / classification
  • Dimerization
  • Escherichia coli Proteins / chemistry*
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Transcription Factors / chemistry*
  • Transcription Factors / classification


  • AbrB protein, Bacillus subtilis
  • Bacterial Proteins
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • MazE protein, E coli
  • Transcription Factors
  • mraZ protein, E coli