Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins |
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Authors: | Bobay Benjamin G Andreeva Antonina Mueller Geoffrey A Cavanagh John Murzin Alexey G |
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Affiliation: | Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, 27695, USA. |
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Abstract: | 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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Keywords: | SCOP, structural classification of proteins CSI, chemical shift indices TALOS, torsion angle likelihood obtained from shift and sequence similarity |
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