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; T. Kwok; D. L. Ollis

doi:10.1016/j.jmb.2006.12.018

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^*, T. Kwok, D. L. Ollis

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

15 Citations (Scopus)

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.

Original language	English
Pages (from-to)	102-112
Number of pages	11
Journal	Journal of Molecular Biology
Volume	367
Issue number	1
DOIs	https://doi.org/10.1016/j.jmb.2006.12.018
Publication status	Published - 16 Mar 2007

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title = "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",

abstract = "The X-ray structure of the N-terminal domain of TyrR has been solved to a resolution of 2.3 {\AA}. 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.",

keywords = "TyrR protein, X-ray structure, activator, repressor, transcription regulation",

author = "D. Verger and Carr, {P. D.} and T. Kwok and Ollis, {D. L.}",

year = "2007",

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doi = "10.1016/j.jmb.2006.12.018",

language = "English",

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journal = "Journal of Molecular Biology",

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T1 - 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

AU - Verger, D.

AU - Carr, P. D.

AU - Kwok, T.

AU - Ollis, D. L.

PY - 2007/3/16

Y1 - 2007/3/16

N2 - 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.

AB - 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.

KW - TyrR protein

KW - X-ray structure

KW - activator

KW - repressor

KW - transcription regulation

UR - http://www.scopus.com/inward/record.url?scp=33847084666&partnerID=8YFLogxK

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DO - 10.1016/j.jmb.2006.12.018

M3 - Article

SN - 0022-2836

VL - 367

SP - 102

EP - 112

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 1

ER -

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

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