3e1k
Crystal structure of Kluyveromyces lactis Gal80p in complex with the acidic activation domain of Gal4pCrystal structure of Kluyveromyces lactis Gal80p in complex with the acidic activation domain of Gal4p
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 PubMedThe GAL genes, which encode the enzymes required for normal galactose metabolism in yeast, are transcriptionally regulated by three proteins: Gal4p, an activator; Gal80p, an inhibitor; and Gal3p, a galactose sensor. These proteins control the switch between inert and active gene expression. The transcriptional activation function of Gal4p is rendered inactive in the presence of Gal80p. Here we present the three-dimensional structure of a complex between the acidic activation domain of Gal4p and Gal80p. The transactivation domain initiates with an extended region of polypeptide chain followed by two turns of an amphipathic alpha-helix. It fits into and across a deep cleft within the Gal80p dimer with the protein-protein interface defined primarily by hydrophobic interactions. A disordered loop in the apo-Gal80p structure (Asp-309 to Ser-316) becomes well-defined upon binding of the transactivation domain. This investigation provides a new molecular scaffold for understanding previous biochemical and genetic studies. The interaction between an acidic transcriptional activator and its inhibitor. The molecular basis of Gal4p recognition by Gal80p.,Thoden JB, Ryan LA, Reece RJ, Holden HM J Biol Chem. 2008 Oct 31;283(44):30266-72. Epub 2008 Aug 13. PMID:18701455[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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