1MI7

Crystal Structure of Domain Swapped trp Aporepressor in 30%(v/v) Isopropanol

Summary for 1MI7

• Entry DOI: 10.2210/pdb1mi7/pdb
• Related: 1TRO 1TRR 1WRP 2WRP 3WRP
• Descriptor: Trp operon repressor, ISOPROPYL ALCOHOL (3 entities in total)
• Functional Keywords: domain swapping, dna binding protein, alcohol induced conformational rearrangement, transcription
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A881
• Total number of polymer chains: 1
• Total formula weight: 12299.03

Authors

Lawson, C.L.,Benoff, B.,Berger, T.,Berman, H.M.,Carey, J. (deposition date: 2002-08-22, release date: 2003-09-02, Last modification date: 2024-02-14)

Primary citation

Lawson, C.L.,Benoff, B.,Berger, T.,Berman, H.M.,Carey, J.
E. coli trp repressor forms a domain-swapped array in aqueous alcohol.
Structure, 12:1099-1108, 2004

PubMed 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.

PubMed: 15274929
DOI: 10.1016/j.str.2004.03.019

Experimental method

X-RAY DIFFRACTION (2.5 Å)