3E1K

Crystal structure of Kluyveromyces lactis Gal80p in complex with the acidic activation domain of Gal4p

Summary for 3E1K

• Entry DOI: 10.2210/pdb3e1k/pdb
• Descriptor: Galactose/lactose metabolism regulatory protein GAL80, Lactose regulatory protein LAC9 (2 entities in total)
• Functional Keywords: transctiption, repressor, trans-activation, carbohydrate metabolism, dna-binding, galactose metabolism, transcription, transcription regulation, activator, metal-binding, nucleus, zinc
• Biological source: Kluyveromyces lactis (yeast); More
• Cellular location: Nucleus: P08657
• Total number of polymer chains: 16
• Total formula weight: 438901.61

Authors

Thoden, J.B.,Holden, H.M. (deposition date: 2008-08-04, release date: 2008-08-12, Last modification date: 2023-08-30)

Primary citation

Thoden, J.B.,Ryan, L.A.,Reece, R.J.,Holden, H.M.
The Interaction between an Acidic Transcriptional Activator and Its Inhibitor: THE MOLECULAR BASIS OF Gal4p RECOGNITION BY Gal80p.
J.Biol.Chem., 283:30266-30272, 2008

PubMed Abstract: The 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.

PubMed: 18701455
DOI: 10.1074/jbc.M805200200

Experimental method

X-RAY DIFFRACTION (3 Å)