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Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex.

Tan S, Richmond TJ
Nature 391 660-6 (1998)
Related entries: 1apl, 1srs

Cited: 166 times
EuropePMC logo PMID: 9490409

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.

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Related citations provided by authors (2)

  1. Structure of serum response factor core bound to DNA.. Pellegrini L, Tan S, Richmond TJ Nature 376 490-8 (1995)
  2. Crystal structure of a MAT alpha 2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions.. Wolberger C, Vershon AK, Liu B, Johnson AD, Pabo CO Cell 67 517-28 (1991)

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