@article{mbs:/content/journal/micro/10.1099/mic.0.2008/022772-0, author = "Maddocks, Sarah E. and Oyston, Petra C. F.", title = "Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins", journal= "Microbiology", year = "2008", volume = "154", number = "12", pages = "3609-3623", doi = "https://doi.org/10.1099/mic.0.2008/022772-0", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.2008/022772-0", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "LTTR, LysR-type transcriptional regulator", keywords = "wHTH, winged-HTH", keywords = "HTH, helix–turn–helix", keywords = "ABS, activation binding site", keywords = "RBS, regulatory binding site", keywords = "DBD, DNA-binding domain", abstract = "The LysR family of transcriptional regulators represents the most abundant type of transcriptional regulator in the prokaryotic kingdom. Members of this family have a conserved structure with an N-terminal DNA-binding helix–turn–helix motif and a C-terminal co-inducer-binding domain. Despite considerable conservation both structurally and functionally, LysR-type transcriptional regulators (LTTRs) regulate a diverse set of genes, including those involved in virulence, metabolism, quorum sensing and motility. Numerous structural and transcriptional studies of members of the LTTR family are helping to unravel a compelling paradigm that has evolved from the original observations and conclusions that were made about this family of transcriptional regulators.", }