Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins.
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.
Bobay
Benjamin G
BG
Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, 27695, USA.
Andreeva
Antonina
A
Mueller
Geoffrey A
GA
Cavanagh
John
J
Murzin
Alexey G
AG
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000378:metabolism; D001426:Bacterial Proteins; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000145:classification; D019281:Dimerization; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D014157:Transcription Factors / Q000737:chemistry* / Q000145:classification
C060762:AbrB protein, Bacillus subtilis; D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C422954:MazE protein, E coli; D014157:Transcription Factors; C104889:mraZ protein, E coli