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Crystal structure of Enterococcus faecalis SlyA-like transcriptional factor.

The crystal structure of a SlyA transcriptional regulator at 1.6 A resolution is presented, and structural relationships between members of the MarR/SlyA family are discussed. The SlyA family, which includes SlyA, Rap, Hor, and RovA proteins, is widely distributed in bacterial and archaeal genomes. Current evidence suggests that SlyA-like factors act as repressors, activators, and modulators of gene transcription. These proteins have been shown to up-regulate the expression of molecular chaperones, acid-resistance proteins, and cytolysin, and down-regulate several biosynthetic enzymes. The structure of SlyA from Enterococcus faecalis, determined as a part of an ongoing structural genomics initiative (www.mcsg.anl.gov), revealed the same winged helix DNA-binding motif that was recently found in the MarR repressor from Escherichia coli and the MexR repressor from Pseudomonas aeruginosa, a sequence homologue of MarR. Phylogenetic analysis of the MarR/SlyA family suggests that Sly is placed between the SlyA and MarR subfamilies and shows significant sequence similarity to members of both subfamilies.[1]

References

  1. Crystal structure of Enterococcus faecalis SlyA-like transcriptional factor. Wu, R.Y., Zhang, R.G., Zagnitko, O., Dementieva, I., Maltzev, N., Watson, J.D., Laskowski, R., Gornicki, P., Joachimiak, A. J. Biol. Chem. (2003) [Pubmed]
 
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