Structural highlights
Function
[TRPR_ECOLI] This protein is an aporepressor. When complexed with L-tryptophan it binds the operator region of the trp operon (5'-ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lawson CL, Benoff B, Berger T, Berman HM, Carey J. E. coli trp repressor forms a domain-swapped array in aqueous alcohol. Structure. 2004 Jun;12(6):1099-108. PMID:15274929 doi:10.1016/j.str.2004.03.019
