1ERJ

CRYSTAL STRUCTURE OF THE C-TERMINAL WD40 DOMAIN OF TUP1

Summary for 1ERJ

• Entry DOI: 10.2210/pdb1erj/pdb
• Descriptor: TRANSCRIPTIONAL REPRESSOR TUP1 (2 entities in total)
• Functional Keywords: beta-propeller, transcription inhibitor
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Nucleus : P16649
• Total number of polymer chains: 3
• Total formula weight: 129924.41

Authors

Sprague, E.R.,Redd, M.J.,Johnson, A.D.,Wolberger, C. (deposition date: 2000-04-06, release date: 2000-07-26, Last modification date: 2024-05-22)

Primary citation

Sprague, E.R.,Redd, M.J.,Johnson, A.D.,Wolberger, C.
Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast.
EMBO J., 19:3016-3027, 2000

PubMed Abstract: The Tup1-Ssn6 corepressor complex regulates the expression of several sets of genes, including genes that specify mating type in the yeast Saccharomyces cerevisiae. Repression of mating-type genes occurs when Tup1-Ssn6 is brought to the DNA by the Matalpha2 DNA-binding protein and assembled upstream of a- and haploid-specific genes. We have determined the 2.3 A X-ray crystal structure of the C-terminal domain of Tup1 (accesion No. 1ERJ), a 43 kDa fragment that contains seven copies of the WD40 sequence motif and binds to the Matalpha2 protein. Moreover, this portion of the protein can partially substitute for full-length Tup1 in bringing about transcriptional repression. The structure reveals a seven-bladed beta propeller with an N-terminal subdomain that is anchored to the side of the propeller and extends the beta sheet of one of the blades. Point mutations in Tup1 that specifically affect the Tup1-Matalpha2 interaction cluster on one surface of the propeller. We identified regions of Tup1 that are conserved among the fungal Tup1 homologs and may be important in protein-protein interactions with additional components of the Tup1-mediated repression pathways.

PubMed: 10856245
DOI: 10.1093/emboj/19.12.3016

Experimental method

X-RAY DIFFRACTION (2.3 Å)