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 X-ray structure of the N-terminal domain of TyrR has been solved to a resolution of 2.3 A. 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 approximately 50 degrees . 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.
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.,Verger D, Carr PD, Kwok T, Ollis DL J Mol Biol. 2007 Mar 16;367(1):102-12. Epub 2006 Dec 12. PMID:17222426[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Verger D, Carr PD, Kwok T, Ollis DL. 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. J Mol Biol. 2007 Mar 16;367(1):102-12. Epub 2006 Dec 12. PMID:17222426 doi:10.1016/j.jmb.2006.12.018
