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FEBS Lett. 2005 Oct 24;579(25):5669-74. Epub 2005 Oct 4.

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

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Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, 27695, USA.


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.

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