Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2188613 | Journal of Molecular Biology | 2007 | 11 Pages |
Abstract
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 ∼50°. 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.
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Authors
D. Verger, P.D. Carr, T. Kwok, D.L. Ollis,