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Structure. 2004 Jun;12(6):1099-108.

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

Author information

  • 1Rutgers University, Department of Chemistry and Chemical Biology, 610 Taylor Road, Piscataway, NJ 08854, USA. cathy.lawson@rutgers.edu

Abstract

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.

PMID:
15274929
[PubMed - indexed for MEDLINE]
PMCID:
PMC3228604
Free PMC Article
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