Download MendeleyCrystal 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.(2003) J Biol Chem 278: 20240-20244
- PubMed: 12649270
- DOI: https://doi.org/10.1074/jbc.M300292200
- Primary Citation of Related Structures:
1LJ9 - PubMed Abstract:
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.
Organizational Affiliation:
Biosciences Division and Structural Biology Center, Argonne National Laboratory, Illinois 60439, USA.
