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Structure of the C-terminal effector-binding domain of AhrC bound to its corepressor L-arginine

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Structure of the C-terminal effector-binding domain of AhrC bound to its corepressor L-arginine. / 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. 918-921.

Research output: Contribution to journalArticle

Harvard

Garnett, JA, Baumberg, S, Stockley, PG & Phillips, SEV 2007, 'Structure of the C-terminal effector-binding domain of AhrC bound to its corepressor L-arginine', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 63, no. 11, pp. 918-921. https://doi.org/10.1107/S1744309107049391

APA

Garnett, J. A., Baumberg, S., Stockley, P. G., & Phillips, S. E. V. (2007). Structure of the C-terminal effector-binding domain of AhrC bound to its corepressor L-arginine. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(11), 918-921. https://doi.org/10.1107/S1744309107049391

Vancouver

Garnett JA, Baumberg S, Stockley PG, Phillips SEV. Structure of the C-terminal effector-binding domain of AhrC bound to its corepressor L-arginine. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2007 Nov 26;63(11):918-921. https://doi.org/10.1107/S1744309107049391

Author

Garnett, James A. ; Baumberg, Simon ; Stockley, Peter G. ; Phillips, Simon E.V. / Structure of the C-terminal effector-binding domain of AhrC bound to its corepressor L-arginine. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2007 ; Vol. 63, No. 11. pp. 918-921.

Bibtex Download

@article{9a3963e6a88e4afe90d7a19e9e1f3b26,
title = "Structure of the C-terminal effector-binding domain of AhrC bound to its corepressor L-arginine",
abstract = "The arginine repressor/activator protein (AhrC) from Bacillus subtilis belongs to a large family of multifunctional transcription factors that are involved in the regulation of bacterial arginine metabolism. AhrC interacts with operator sites in the promoters of arginine biosynthetic and catabolic operons, acting as a transcriptional repressor at biosynthetic sites and an activator of transcription at catabolic sites. AhrC is a hexamer of identical subunits, each having two domains. The C-terminal domains form the core of the protein and are involved in oligomerization and l-arginine binding. The N-terminal domains lie on the outside of the compact core and play a role in binding to 18 bp DNA operators called ARG boxes. The C-terminal domain of AhrC has been expressed, purified and characterized, and also crystallized as a hexamer with the bound corepressor l-arginine. Here, the crystal structure refined to 1.95 {\AA} is presented.",
keywords = "AhrC, Arginine metabolism, Transcription factors",
author = "Garnett, {James A.} and Simon Baumberg and Stockley, {Peter G.} and Phillips, {Simon E.V.}",
year = "2007",
month = "11",
day = "26",
doi = "10.1107/S1744309107049391",
language = "English",
volume = "63",
pages = "918--921",
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 - Structure of the C-terminal effector-binding domain of AhrC bound to its corepressor L-arginine

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 - The arginine repressor/activator protein (AhrC) from Bacillus subtilis belongs to a large family of multifunctional transcription factors that are involved in the regulation of bacterial arginine metabolism. AhrC interacts with operator sites in the promoters of arginine biosynthetic and catabolic operons, acting as a transcriptional repressor at biosynthetic sites and an activator of transcription at catabolic sites. AhrC is a hexamer of identical subunits, each having two domains. The C-terminal domains form the core of the protein and are involved in oligomerization and l-arginine binding. The N-terminal domains lie on the outside of the compact core and play a role in binding to 18 bp DNA operators called ARG boxes. The C-terminal domain of AhrC has been expressed, purified and characterized, and also crystallized as a hexamer with the bound corepressor l-arginine. Here, the crystal structure refined to 1.95 Å is presented.

AB - The arginine repressor/activator protein (AhrC) from Bacillus subtilis belongs to a large family of multifunctional transcription factors that are involved in the regulation of bacterial arginine metabolism. AhrC interacts with operator sites in the promoters of arginine biosynthetic and catabolic operons, acting as a transcriptional repressor at biosynthetic sites and an activator of transcription at catabolic sites. AhrC is a hexamer of identical subunits, each having two domains. The C-terminal domains form the core of the protein and are involved in oligomerization and l-arginine binding. The N-terminal domains lie on the outside of the compact core and play a role in binding to 18 bp DNA operators called ARG boxes. The C-terminal domain of AhrC has been expressed, purified and characterized, and also crystallized as a hexamer with the bound corepressor l-arginine. Here, the crystal structure refined to 1.95 Å is presented.

KW - AhrC

KW - Arginine metabolism

KW - Transcription factors

UR - http://www.scopus.com/inward/record.url?scp=36248935526&partnerID=8YFLogxK

U2 - 10.1107/S1744309107049391

DO - 10.1107/S1744309107049391

M3 - Article

C2 - 18007040

AN - SCOPUS:36248935526

VL - 63

SP - 918

EP - 921

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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