3V2U
Crystal structure of the yeast GAL regulon complex of the repressor, Gal80p, and the transducer, Gal3p, with galactose and ATP
Summary for 3V2U
Entry DOI | 10.2210/pdb3v2u/pdb |
Related | 2AJ4 3BTS 3BTU 3BTV 3V5R |
Descriptor | Galactose/lactose metabolism regulatory protein GAL80, Protein GAL3, GLYCEROL, ... (7 entities in total) |
Functional Keywords | rossmann fold, ghmp superfamily, transcription regulation, transcription |
Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
Total number of polymer chains | 4 |
Total formula weight | 215223.57 |
Authors | Lavy, T.,Kumar, P.R.,He, H.,Joshua-Tor, L. (deposition date: 2011-12-12, release date: 2012-02-08, Last modification date: 2023-09-13) |
Primary citation | Lavy, T.,Kumar, P.R.,He, H.,Joshua-Tor, L. The Gal3p transducer of the GAL regulon interacts with the Gal80p repressor in its ligand-induced closed conformation. Genes Dev., 26:294-303, 2012 Cited by PubMed Abstract: A wealth of genetic information and some biochemical analysis have made the GAL regulon of the yeast Saccharomyces cerevisiae a classic model system for studying transcriptional activation in eukaryotes. Galactose induces this transcriptional switch, which is regulated by three proteins: the transcriptional activator Gal4p, bound to DNA; the repressor Gal80p; and the transducer Gal3p. We showed previously that NADP appears to act as a trigger to kick the repressor off the activator. Sustained activation involves a complex of the transducer Gal3p and Gal80p mediated by galactose and ATP. We solved the crystal structure of the complex of Gal3p-Gal80p with α-D-galactose and ATP to 2.1 Å resolution. The interaction between the proteins occurs only when Gal3p is in a "closed" state induced by ligand binding. The structure of the complex provides a rationale for the phenotypes of several well-known Gal80p and Gal3p mutants as well as the lack of galactokinase activity of Gal3p. PubMed: 22302941DOI: 10.1101/gad.182691.111 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.105 Å) |
Structure validation
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