Crystal structure of enterococcus faecalis sly A-like transcriptional factor.
The crystal structure of a SlyA transcriptional regulator at 1.6 {angstrom} 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.
- Research Organization:
- Argonne National Laboratory (ANL)
- Sponsoring Organization:
- NIH; SC
- DOE Contract Number:
- AC02-06CH11357
- OSTI ID:
- 961283
- Report Number(s):
- ANL/BIO/JA-46198
- Journal Information:
- J. Biol. Chem., Journal Name: J. Biol. Chem. Journal Issue: 22 ; May 30, 2003 Vol. 278; ISSN JBCHA3; ISSN 0021-9258
- Country of Publication:
- United States
- Language:
- ENGLISH
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