1mi7

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Image:1mi7.gif

1mi7, resolution 2.50Å

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

Overview

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.

About this Structure

1MI7 is a Single protein structure of sequence from Escherichia coli with IPA as ligand. Full crystallographic information is available from OCA.

Reference

E. coli trp repressor forms a domain-swapped array in aqueous alcohol., Lawson CL, Benoff B, Berger T, Berman HM, Carey J, Structure. 2004 Jun;12(6):1099-108. PMID:15274929

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