Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins
Bobay, B. G., Andreeva, A., Mueller, G. A., Cavanagh, J., & Murzin, A. G. (2005). Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins. FEBS Letters, 579(25), 5669-5674. DOI: 10.1016/j.febslet.2005.09.045
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. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.