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A high-resolution structure of the DNA-binding domain of AhrC, the arginine repressor/activator protein from Bacillus subtilis

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A high-resolution structure of the DNA-binding domain of AhrC, the arginine repressor/activator protein from Bacillus subtilis. / Garnett, James A.; Baumberg, Simon; Stockley, Peter G.; Phillips, Simon E.V.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 63, No. 11, 26.11.2007, p. 914-917.

Research output: Contribution to journalArticlepeer-review

Harvard

Garnett, JA, Baumberg, S, Stockley, PG & Phillips, SEV 2007, 'A high-resolution structure of the DNA-binding domain of AhrC, the arginine repressor/activator protein from Bacillus subtilis', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 63, no. 11, pp. 914-917. https://doi.org/10.1107/S1744309107048166

APA

Garnett, J. A., Baumberg, S., Stockley, P. G., & Phillips, S. E. V. (2007). A high-resolution structure of the DNA-binding domain of AhrC, the arginine repressor/activator protein from Bacillus subtilis. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(11), 914-917. https://doi.org/10.1107/S1744309107048166

Vancouver

Garnett JA, Baumberg S, Stockley PG, Phillips SEV. A high-resolution structure of the DNA-binding domain of AhrC, the arginine repressor/activator protein from Bacillus subtilis. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2007 Nov 26;63(11):914-917. https://doi.org/10.1107/S1744309107048166

Author

Garnett, James A. ; Baumberg, Simon ; Stockley, Peter G. ; Phillips, Simon E.V. / A high-resolution structure of the DNA-binding domain of AhrC, the arginine repressor/activator protein from Bacillus subtilis. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2007 ; Vol. 63, No. 11. pp. 914-917.

Bibtex Download

@article{96bee64927dd423d871bedd029cfdfcc,
title = "A high-resolution structure of the DNA-binding domain of AhrC, the arginine repressor/activator protein from Bacillus subtilis",
abstract = "In Bacillus subtilis the concentration of l-arginine is controlled by the transcriptional regulator AhrC, which interacts with 18 bp DNA operator sites called ARG boxes in the promoters of arginine biosynthetic and catabolic operons. AhrC is a 100 kDa homohexamer, with each subunit having two domains. The C-terminal domains form the core, mediating intersubunit interactions and binding of the co-repressor l-arginine, whilst the N-terminal domains contain a winged helix-turn-helix DNA-binding motif and are arranged around the periphery. The N-terminal domain of AhrC has been expressed, purified and characterized and it has been shown that the fragment still binds DNA operators as a recombinant monomer. The DNA-binding domain has also been crystallized and the crystal structure refined to 1.0 {\AA} resolution is presented.",
keywords = "AhrC, Arginine repressor/activator protein, DNA-binding domain",
author = "Garnett, {James A.} and Simon Baumberg and Stockley, {Peter G.} and Phillips, {Simon E.V.}",
year = "2007",
month = nov,
day = "26",
doi = "10.1107/S1744309107048166",
language = "English",
volume = "63",
pages = "914--917",
journal = "Acta Crystallographica Section F-Structural Biology And Crystallization Communications",
issn = "1744-3091",
publisher = "Wiley-Blackwell",
number = "11",

}

RIS (suitable for import to EndNote) Download

TY - JOUR

T1 - A high-resolution structure of the DNA-binding domain of AhrC, the arginine repressor/activator protein from Bacillus subtilis

AU - Garnett, James A.

AU - Baumberg, Simon

AU - Stockley, Peter G.

AU - Phillips, Simon E.V.

PY - 2007/11/26

Y1 - 2007/11/26

N2 - In Bacillus subtilis the concentration of l-arginine is controlled by the transcriptional regulator AhrC, which interacts with 18 bp DNA operator sites called ARG boxes in the promoters of arginine biosynthetic and catabolic operons. AhrC is a 100 kDa homohexamer, with each subunit having two domains. The C-terminal domains form the core, mediating intersubunit interactions and binding of the co-repressor l-arginine, whilst the N-terminal domains contain a winged helix-turn-helix DNA-binding motif and are arranged around the periphery. The N-terminal domain of AhrC has been expressed, purified and characterized and it has been shown that the fragment still binds DNA operators as a recombinant monomer. The DNA-binding domain has also been crystallized and the crystal structure refined to 1.0 Å resolution is presented.

AB - In Bacillus subtilis the concentration of l-arginine is controlled by the transcriptional regulator AhrC, which interacts with 18 bp DNA operator sites called ARG boxes in the promoters of arginine biosynthetic and catabolic operons. AhrC is a 100 kDa homohexamer, with each subunit having two domains. The C-terminal domains form the core, mediating intersubunit interactions and binding of the co-repressor l-arginine, whilst the N-terminal domains contain a winged helix-turn-helix DNA-binding motif and are arranged around the periphery. The N-terminal domain of AhrC has been expressed, purified and characterized and it has been shown that the fragment still binds DNA operators as a recombinant monomer. The DNA-binding domain has also been crystallized and the crystal structure refined to 1.0 Å resolution is presented.

KW - AhrC

KW - Arginine repressor/activator protein

KW - DNA-binding domain

UR - http://www.scopus.com/inward/record.url?scp=36248966191&partnerID=8YFLogxK

U2 - 10.1107/S1744309107048166

DO - 10.1107/S1744309107048166

M3 - Article

C2 - 18007039

AN - SCOPUS:36248966191

VL - 63

SP - 914

EP - 917

JO - Acta Crystallographica Section F-Structural Biology And Crystallization Communications

JF - Acta Crystallographica Section F-Structural Biology And Crystallization Communications

SN - 1744-3091

IS - 11

ER -

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