Verger, Denis and Carr, P.D. and Kwok, T. and Ollis, D.L. (2007) Crystal structure of the N-terminal domain of the TyrR transcription factor responsible for gene regulation of aromatic amino acid biosynthesis and transport in Escherichia coli K12. Journal of Molecular Biology 367 (1), 102 - 112. ISSN 0022-2836.Full text not available from this repository.
The X-ray structure of the N-terminal domain of TyrR has been solved to a resolution of 2.3 Å. It reveals a modular protein containing an ACT domain, a connecting helix, a PAS domain and a C-terminal helix. Two dimers are present in the asymmetric unit with one monomer of each pair exhibiting a large rigid-body movement that results in a hinging around residue 74 of not, vert, similar50°. The structure of the dimer is discussed with reference to other transcription regulator proteins. Putative binding sites are identified for the aromatic amino acid cofactors.
|Keyword(s) / Subject(s):||TyrR protein, transcription regulation, repressor, activator, X-ray structure|
|School or Research Centre:||Birkbeck Schools and Research Centres > School of Science > Biological Sciences|
|Date Deposited:||08 Aug 2011 11:10|
|Last Modified:||17 Apr 2013 12:21|
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