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

D Verger, P D Carr, Terry Kwok, D L Ollis

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10 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)102 - 112
Number of pages11
JournalJournal of Molecular Biology
Volume367
Issue number1
Publication statusPublished - 2007
Externally publishedYes

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