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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 DOI10.2210/pdb3v2u/pdb
Related2AJ4 3BTS 3BTU 3BTV 3V5R
DescriptorGalactose/lactose metabolism regulatory protein GAL80, Protein GAL3, GLYCEROL, ... (7 entities in total)
Functional Keywordsrossmann fold, ghmp superfamily, transcription regulation, transcription
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
More
Total number of polymer chains4
Total formula weight215223.57
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 citationLavy, 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: 22302941
DOI: 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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数据于2025-06-18公开中

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