1LJ9

The crystal structure of the transcriptional regulator SlyA

Summary for 1LJ9

• Entry DOI: 10.2210/pdb1lj9/pdb
• Descriptor: transcriptional regulator SlyA (2 entities in total)
• Functional Keywords: hth dna binding protein, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, transcription
• Biological source: Enterococcus faecalis
• Total number of polymer chains: 2
• Total formula weight: 33364.36

Authors

Wu, R.Y.,Zhang, R.G.,Gornicki, P.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2002-04-19, release date: 2003-01-21, Last modification date: 2024-02-14)

Primary citation

Wu, R.Y.,Zhang, R.G.,Zagnitko, O.,Dementieva, I.,Maltzev, N.,Watson, J.D.,Laskowski, R.,Gornicki, P.,Joachimiak, A.
Crystal structure of Enterococcus faecalis SlyA-like transcriptional factor
J.Biol.Chem., 278:20240-20244, 2003

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.

PubMed: 12649270
DOI: 10.1074/jbc.M300292200

Experimental method

X-RAY DIFFRACTION (1.6 Å)