3VP9

Crystal structure of the N-terminal domain of the yeast general corepressor Tup1p mutant

Summary for 3VP9

• Entry DOI: 10.2210/pdb3vp9/pdb
• Related: 3VP8
• Descriptor: General transcriptional corepressor TUP1, 1,4-DIETHYLENE DIOXIDE (3 entities in total)
• Functional Keywords: four helix bundle, transcription
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Nucleus: P16649
• Total number of polymer chains: 2
• Total formula weight: 22525.25

Authors

Matsumura, H.,Kusaka, N.,Nakamura, T.,Tanaka, N.,Sagegami, K.,Uegaki, K.,Inoue, T.,Mukai, Y. (deposition date: 2012-02-28, release date: 2012-06-13, Last modification date: 2024-03-20)

Primary citation

Matsumura, H.,Kusaka, N.,Nakamura, T.,Tanaka, N.,Sagegami, K.,Uegaki, K.,Inoue, T.,Mukai, Y.
Crystal structure of the N-terminal domain of the yeast general corepressor Tup1p and its functional implications
J.Biol.Chem., 287:26528-26538, 2012

PubMed Abstract: The yeast Cyc8p-Tup1p protein complex is a general transcriptional corepressor of genes involved in many different physiological processes. Herein, we present the crystal structure of the Tup1p N-terminal domain (residues 1-92), essential for Tup1p self-assembly and interaction with Cyc8p. This domain tetramerizes to form a novel antiparallel four-helix bundle. Coiled coil interactions near the helical ends hold each dimer together, whereas interdimeric association involves only two sets of two residues located toward the chain centers. A mutagenesis study confirmed that the nonpolar residues responsible for the association of the protomers as dimers are also required for transcriptional repression. An additional structural study demonstrated that the domain containing an Leu(62) → Arg mutation that had been shown not to bind Cyc8p exhibits an altered structure, distinct from the wild type. This altered structure explains why the mutant cannot bind Cyc8p. The data presented herein highlight the importance of the architecture of the Tup1p N-terminal domain for self-association.

PubMed: 22707714
DOI: 10.1074/jbc.M112.369652

Experimental method

X-RAY DIFFRACTION (1.799 Å)