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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

Date

Authors

Verger, Denis

Carr, Paul D

Kwok, Terry

Ollis, David

Publisher

Elsevier

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

Keywords

Keywords: aromatic amino acid; dimer; monomer; protein subunit; regulator protein; transcription factor; transcription factor TyrR; unclassified drug; amino acid synthesis; amino acid transport; amino terminal sequence; article; binding site; carboxy terminal seque activator; repressor; transcription regulation; TyrR protein; X-ray structure

URI

http://hdl.handle.net/1885/24893

Collections

Open Access Research

Source

Journal of Molecular Biology

Type

Journal article

DOI

10.1016/j.jmb.2006.12.018

Restricted until

2037-12-31

Downloads

File

Description

01_Verger_Crystal_structure_of_the_2007.pdf (1.68 MB)