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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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 A 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.[1]

References

  1. E. coli trp repressor forms a domain-swapped array in aqueous alcohol. Lawson, C.L., Benoff, B., Berger, T., Berman, H.M., Carey, J. Structure (Camb.) (2004) [Pubmed]
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