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Crystal structure of the yeast MATα2/MCM1/DNA ternary complex

Nature volume 391, pages 660–666 (1998)Cite this article

Abstract

The structure of a complex containing the homeodomain repressor protein MATα2 and the MADS-box transcription factor MCM1 bound to DNA has been determined by X-ray crystallography at 2.25 Å resolution. It reveals the protein–protein interactions responsible for cooperative binding of MATα2 and MCM1 to DNA. The otherwise flexible amino-terminal extension of the MATα2 homeodomain forms a β-hairpin that grips the MCM1 surface through parallel β-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 α-helical conformation in one of two copies of the MATα2 monomer and a β-strand conformation in the other. This ‘chameleon’ sequence of MATα2 may be important for recognizing natural operator sites.

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Figure 1: Structure of the α2/MCM1/STE6 DNA complex.
Figure 2: Details of MCM1–DNA interactions and electron density of chameleon sequences.
Figure 3: α2–MCM1 interactions.
Figure 4: Model for the interaction of α2 and MCM1 on 31 bp of STE6 UAS.

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Acknowledgements

We thank Y. Hunziker, L. Pellegrini and D. Sargent for their support and assistance, and A. Thompson at BM14 of the ESRF Grenoble for help during data collection. This research was supported in part by the Swiss National Science Foundation.

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  1. ETH-Zürich, Institut för Molekularbiologie und Biophysik, ETH-Hönggerberg, CH-8093, Zürich, Switzerland

    Song Tan & Timothy J. Richmond

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Tan, S., Richmond, T. Crystal structure of the yeast MATα2/MCM1/DNA ternary complex. Nature 391, 660–666 (1998). https://doi.org/10.1038/35563

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