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, 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.

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Official URL: http://dx.doi.org/10.1016/j.jmb.2006.12.018

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 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.

Metadata

Item Type:	Article
Keyword(s) / Subject(s):	TyrR protein, transcription regulation, repressor, activator, X-ray structure
School:	Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
Depositing User:	Administrator
Date Deposited:	08 Aug 2011 11:10
Last Modified:	02 Aug 2023 16:55
URI:	https://eprints.bbk.ac.uk/id/eprint/3974

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