1erj
From Proteopedia
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CRYSTAL STRUCTURE OF THE C-TERMINAL WD40 DOMAIN OF TUP1
Overview
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.
About this Structure
1ERJ is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast., Sprague ER, Redd MJ, Johnson AD, Wolberger C, EMBO J. 2000 Jun 15;19(12):3016-27. PMID:10856245
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