PMID:15274929

Citation	Lawson, CL, Benoff, B, Berger, T, Berman, HM and Carey, J (2004) E. coli trp repressor forms a domain-swapped array in aqueous alcohol. Structure 12:1099-108
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.
Links	PubMed PMC3228604 Online version:10.1016/j.str.2004.03.019
Keywords	2-Propanol/chemistry; Alcohols/chemistry; Amino Acid Motifs; Amino Acid Sequence; Animals; Bacterial Proteins/chemistry; Binding Sites; Crystallography, X-Ray; Dimerization; Escherichia coli/metabolism; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Repressor Proteins/chemistry; Scattering, Radiation; X-Rays
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