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PDBsum entry 1erj

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Top Page protein Protein-protein interface(s) links
Transcription inhibitor PDB id
1erj
Contents
Protein chains
350 a.a. *
Waters ×265
* Residue conservation analysis

References listed in PDB file
Key reference
Title Structure of the c-Terminal domain of tup1, A corepressor of transcription in yeast.
Authors E.R.Sprague, M.J.Redd, A.D.Johnson, C.Wolberger.
Ref. EMBO J, 2000, 19, 3016-3027. [DOI no: 10.1093/emboj/19.12.3016]
PubMed id 10856245
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.
Figure 2.
Figure 2 Packing of the N-terminal fragment against the propeller. (A) Extended sheet formed by blade 6 and strands n1 and n2 from the N-terminal fragment. Hydrogen bonds are indicated with dashed lines. (B) Stereoview of contacts between the N-terminal fragment (283–331) and the propeller. Side chain and backbone atoms are superimposed on the C[ ]trace. Some side chain labels were omitted for clarity. The approximate boundaries of each blade are shown in different colors (blade 5, light green; blade 6, blue; blade 7, red; N-terminal fragment, gray). This figure was generated with RIBBONS (Carson, 1997).
Figure 3.
Figure 3 (A) Superposition of all seven blades of Tup1. The C[ ]backbone for each of the seven blades was aligned with respect to strands 3B and 3C. The four conserved side chains involved in the intrablade hydrogen-bonding network, referred to as the structural tetrad, are shown for blade 3 as ball-and-stick models colored according to atom type and hydrogen bonds are indicated with dashed lines. A representative blade from G , blade 4, is shown for reference. Blade 1, light green; blade 2, red; blade 3, green; blade 4, purple; blade 5, pink; blade 6, cyan; blade 7, orange; G , brown. (B) Superposition of the WD40 propellers. The C[ ]backbones for G (blue; 1TBG) and Tup1 (yellow), which align with an r.m.s.d. of 1.3 Å, are shown in the same view as Figure 1A and labeled. Least-squares alignments for (A) and (B) were done in O (Jones et al., 1991) and figures generated with RIBBONS (Carson, 1997).
The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2000, 19, 3016-3027) copyright 2000.
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