1MNM

YEAST MATALPHA2/MCM1/DNA TERNARY TRANSCRIPTION COMPLEX CRYSTAL STRUCTURE

Summary for 1MNM

• Entry DOI: 10.2210/pdb1mnm/pdb
• Descriptor: DNA (STE6 OPERATOR DNA), PROTEIN (MCM1 TRANSCRIPTIONAL REGULATOR), PROTEIN (MAT ALPHA-2 TRANSCRIPTIONAL REPRESSOR), ... (5 entities in total)
• Functional Keywords: transcription regulation, transcriptional repression, dna-binding protein, complex (transcription-homeobox-dna), transcription-dna complex, transcription/dna
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Nucleus: P11746
• Total number of polymer chains: 6
• Total formula weight: 59447.16

Authors

Tan, S.,Richmond, T.J. (deposition date: 1997-11-03, release date: 1998-03-18, Last modification date: 2023-08-02)

Primary citation

Tan, S.,Richmond, T.J.
Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex.
Nature, 391:660-666, 1998

PubMed Abstract: The structure of a complex containing the homeodomain repressor protein MATalpha2 and the MADS-box transcription factor MCM1 bound to DNA has been determined by X-ray crystallography at 2.25 A resolution. It reveals the protein-protein interactions responsible for cooperative binding of MATalpha2 and MCM1 to DNA. The otherwise flexible amino-terminal extension of the MATalpha2 homeodomain forms a beta-hairpin that grips the MCM1 surface through parallel beta-strand hydrogen bonds and close-packed, predominantly hydrophobic, side chains. DNA bending induced by MCM1 brings the two proteins closer together, facilitating their interaction. An unusual feature of the complex is that an eight-amino-acid sequence adopts an alpha-helical conformation in one of two copies of the MATalpha2 monomer and a beta-strand conformation in the other. This 'chameleon' sequence of MATalpha2 may be important for recognizing natural operator sites.

PubMed: 9490409
DOI: 10.1038/35563

Experimental method

X-RAY DIFFRACTION (2.25 Å)