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The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils

Nature Structural Biology volume 6, pages 755–759 (1999)Cite this article

Abstract

The tetrameric Mnt repressor is involved in the genetic switch between the lysogenic and lytic growth of Salmonella bacteriophage P22. The solution structure of its C-terminal tetramerization domain, which holds together the two dimeric DNA-binding domains, has been determined by NMR spectroscopy. This structure reveals an assembly of four α-helical subunits, consisting of a dimer of two antiparallel coiled coils with a unique right-handed twist. The superhelical winding is considerably stronger and the interhelical separation closer than those found in the well-known left-handed coiled coils in fibrous proteins and leucine zippers. An unusual asymmetry arises between the two monomers that comprise one right-handed coiled coil. A difference in the packing to the adjacent monomer of the other coiled coil occurs with an offset of two helical turns. The two asymmetric monomers within each coiled coil interconvert on a time scale of seconds. Both with respect to symmetry and handedness of helical packing, the C2 symmetric four-helix bundle of Mnt differs from other oligomerization domains that assemble DNA-binding modules, such as that in the tumor suppressor p53 and the E. coli lac repressor.

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Figure 1: NMR data on Mnt-C.
Figure 2: Views of the Mnt-C structure.
Figure 3: Interhelical packing in the Mnt-C tetramer.
Figure 4: Comparison of the C2 symmetric Mnt-C four-helix bundle to these of the D2 symmetric tetramerization domains of lac repressor and p53, and to the four-helix bundle of yeast TFIIA with a right-handed superhelix.

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Acknowledgements

This research was supported by the Council of Earth and Life Sciences of the Netherlands Organization for Scientific Research (ALW/NWO). We thank A.George and C. Waldburger for their help in protein expression and purification. D. Walther is gratefully acknowledged for his help in the analysis of helical parameters.

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Authors and Affiliations

  1. Department of NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, Utrecht, 3584 CH, The Netherlands

    Irene M.A. Nooren, Robert Kaptein & Rolf Boelens

  2. Department of Biology, Massachusetts Institute of Technology, Cambridge, 02139, Massachusetts, USA

    Robert T. Sauer

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  1. Irene M.A. Nooren
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  2. Robert Kaptein
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  3. Robert T. Sauer
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  4. Rolf Boelens
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Correspondence to Rolf Boelens.

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Nooren, I., Kaptein, R., Sauer, R. et al. The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils. Nat Struct Mol Biol 6, 755–759 (1999). https://doi.org/10.1038/11531

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