E. coli trp repressor forms a domain-swapped array in aqueous alcohol

Catherine L. Lawson, Brian Benoff, Tatyana Berger, Helen M. Berman, Jannette Carey

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


The E. coli trp repressor (trpR) homodimer recognizes its palindromic DNA binding site through a pair of flexible helix-turn-helix (HTH) motifs displayed on an intertwined helical core. Flexible N-terminal arms mediate association between dimers bound to tandem DNA sites. The 2.5 Å X-ray structure of trpR crystallized in 30% (v/v) isopropanol reveals a substantial conformational rearrangement of HTH motifs and N-terminal arms, with the protein appearing in the unusual form of an ordered 3D domain-swapped supramolecular array. Small angle X-ray scattering measurements show that the self-association properties of trpR in solution are fundamentally altered by isopropanol.

Original languageEnglish (US)
Pages (from-to)1099-1108
Number of pages10
Issue number6
StatePublished - Jun 2004

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Structural Biology


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