2NVW

Crystal sctucture of transcriptional regulator Gal80p from kluyveromymes lactis

Summary for 2NVW

• Entry DOI: 10.2210/pdb2nvw/pdb
• Descriptor: Galactose/lactose metabolism regulatory protein GAL80 (2 entities in total)
• Functional Keywords: transcription, galactose metabolism, repressor
• Biological source: Kluyveromyces lactis
• Total number of polymer chains: 2
• Total formula weight: 107286.95

Authors

Thoden, J.B.,Sellick, C.A.,Reece, R.J.,Holden, H.M. (deposition date: 2006-11-13, release date: 2006-11-21, Last modification date: 2023-12-27)

Primary citation

Thoden, J.B.,Sellick, C.A.,Reece, R.J.,Holden, H.M.
Understanding a transcriptional paradigm at the molecular level. The structure of yeast Gal80p.
J.Biol.Chem., 282:1534-1538, 2007

PubMed Abstract: In 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.

PubMed: 17121853
DOI: 10.1074/jbc.C600285200

Experimental method

X-RAY DIFFRACTION (2.1 Å)