title: Crystal structure of Enterococcus faecalis SlyA-like transcriptional factor.
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.
authors.affiliation: Biosciences Division and Structural Biology Center, Argonne National Laboratory, Illinois 60439, USA.
authors.forename: Rui-ying
authors.initials: RY
authors.lastname: Wu
authors.forename: Rong-guang
authors.initials: RG
authors.lastname: Zhang
authors.forename: Olga
authors.initials: O
authors.lastname: Zagnitko
authors.forename: Irina
authors.initials: I
authors.lastname: Dementieva
authors.forename: Natalia
authors.initials: N
authors.lastname: Maltzev
authors.forename: James D
authors.initials: JD
authors.lastname: Watson
authors.forename: Roman
authors.initials: R
authors.lastname: Laskowski
authors.forename: Piotr
authors.initials: P
authors.lastname: Gornicki
authors.forename: Andrzej
authors.initials: A
authors.lastname: Joachimiak
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001427:Bacterial Toxins / Q000737:chemistry* / Q000378:metabolism; D004269:DNA, Bacterial / Q000378:metabolism; D013293:Enterococcus faecalis / Q000737:chemistry* / Q000378:metabolism; D006460:Hemolysin Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010802:Phylogeny; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors
chemical_list: D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004269:DNA, Bacterial; D006460:Hemolysin Proteins; D014157:Transcription Factors; C056785:salmolysin