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Crystal sctucture of transcriptional regulator Gal80p from kluyveromymes lactisCrystal sctucture of transcriptional regulator Gal80p from kluyveromymes lactis
Structural highlights
FunctionGAL80_KLULA This protein is a negative regulator for the gene expression of the lactose/galactose metabolic genes. It seems to block activation by the transcriptional activator LAC9 in the absence of an inducing sugar. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn yeast, the GAL genes encode the enzymes required for normal galactose metabolism. Regulation of these genes in response to the organism being challenged with galactose has served as a paradigm for eukaryotic transcriptional control over the last 50 years. Three proteins, the activator Gal4p, the repressor Gal80p, and the ligand sensor Gal3p, control the switch between inert and active gene expression. Gal80p, the focus of this investigation, plays a pivotal role both in terms of repressing the activity of Gal4p and allowing the GAL switch to respond to galactose. Here we present the three-dimensional structure of Gal80p from Kluyveromyces lactis and show that it is structurally homologous to glucose-fructose oxidoreductase, an enzyme in the sorbitol-gluconate pathway. Our results clearly define the overall tertiary and quaternary structure of Gal80p and suggest that Gal4p and Gal3p bind to Gal80p at distinct but overlapping sites. In addition to providing a molecular basis for previous biochemical and genetic studies, our structure demonstrates that much of the enzymatic scaffold of the oxidoreductase has been maintained in Gal80p, but it is utilized in a very different manner to facilitate transcriptional regulation. Understanding a transcriptional paradigm at the molecular level. The structure of yeast Gal80p.,Thoden JB, Sellick CA, Reece RJ, Holden HM J Biol Chem. 2007 Jan 19;282(3):1534-8. Epub 2006 Nov 22. PMID:17121853[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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