title: Defying stereotypes: the elusive search for a universal model of LysR-type regulation.
abstract: LysR-type transcriptional regulators (LTTRs) compose the largest family of homologous regulators in bacteria. Considering their prevalence, it is not surprising that LTTRs control diverse metabolic functions. Arguably, the most unexpected aspect of LTTRs is the paucity of available structural information. Solubility issues are notoriously problematic, and structural studies have only recently begun to flourish. In this issue of Molecular Microbiology, Taylor et al. (2012) present the structure of AphB, a LysR-type regulator of virulence in Vibrio cholerae. This contribution adds significantly to the group of known full-length atomic LTTR structures, which remains small. Importantly, this report also describes an active-form variant. Small conformational changes in the effector-binding domain translate to global reorganization of the DNA-binding domain. Emerging from these results is a model of theme-and-variation among LTTRs rather than a unified regulatory scheme. Despite common structural folds, LTTRs exhibit differences in oligomerization, promoter recognition and communication with RNA polymerase. Such variation mirrors the diversity in sequence and function associated with members of this very large family.
authors.affiliation: Departments of Pharmaceutical and Biomedical Sciences Microbiology, University of Georgia, Athens, GA 30602, USA. cmomany@rx.uga.edu;
authors.forename: Cory
authors.initials: C
authors.lastname: Momany
authors.forename: Ellen L
authors.initials: EL
authors.lastname: Neidle
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D010100:Oxygen / Q000737:chemistry*; D015534:Trans-Activators / Q000737:chemistry*; D014734:Vibrio cholerae / Q000737:chemistry*
chemical_list: C120327:AphB protein, Vibrio cholerae; D001426:Bacterial Proteins; D015534:Trans-Activators; D010100:Oxygen