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

I.M.A. Nooren, R. Kaptein, R.T. Sauer, R. Boelens

Research output: Contribution to journalArticleAcademicpeer-review


The tetrameric Mnt repressor is involved in the genetic switch between the lysogenic and lyric 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 C2symmetric 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.
Original languageEnglish
Pages (from-to)755-759
Number of pages5
JournalNature Structural Biology
Issue number8
Publication statusPublished - 8 Sept 1999


  • peptide
  • tetramer
  • alpha helix
  • article
  • carboxy terminal sequence
  • DNA binding
  • molecular model
  • nuclear magnetic resonance spectroscopy
  • oligomerization
  • priority journal
  • protein domain
  • protein structure
  • structure analysis


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