Purification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3]

Xavier Jean Philippe Kubiak; Benjamin Pluvinage; Inès Li de la Sierra-Gallay; Patrick Weber; Ahmed Haouz; Jean-Marie Dupret; Fernando Rodrigues-Lima

doi:10.1107/S1744309111053942

Purification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3]

Xavier Jean Philippe Kubiak, Benjamin Pluvinage, Inès Li de la Sierra-Gallay, Patrick Weber, Ahmed Haouz, Jean-Marie Dupret, Fernando Rodrigues-Lima

Institut for Neurovidenskab

5 Citationer (Scopus)

Abstract

Arylamine N-acetyltransferases (NATs) are xenobiotic metabolizing enzymes (XMEs) that catalyze the acetylation of arylamines. All functional NATs described to date possess a strictly conserved Cys-His-Asp catalytic triad. Here, the purification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3], a putative NAT isoenzyme that possesses a unique catalytic triad containing a glutamate residue, is reported. The crystal diffracted to 2.42 Å resolution and belonged to the monoclinic space group C121, with unit-cell parameters a = 90.44, b = 44.52, c = 132.98 Å, β = 103.8°.

Originalsprog	Engelsk
Tidsskrift	Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online
Vol/bind	68
Udgave nummer	Pt 2
Sider (fra-til)	196-8
Antal sider	3
ISSN	1744-3091
DOI	https://doi.org/10.1107/S1744309111053942
Status	Udgivet - 1 feb. 2012

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10.1107/S1744309111053942

Citationsformater

Kubiak, X. J. P., Pluvinage, B., Li de la Sierra-Gallay, I., Weber, P., Haouz, A., Dupret, J-M., & Rodrigues-Lima, F. (2012). Purification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3]. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 68(Pt 2), 196-8. https://doi.org/10.1107/S1744309111053942

Purification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3]. / Kubiak, Xavier Jean Philippe; Pluvinage, Benjamin; Li de la Sierra-Gallay, Inès et al.

I: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, Bind 68, Nr. Pt 2, 01.02.2012, s. 196-8.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

Kubiak, XJP, Pluvinage, B, Li de la Sierra-Gallay, I, Weber, P, Haouz, A, Dupret, J-M & Rodrigues-Lima, F 2012, 'Purification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3]', Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, bind 68, nr. Pt 2, s. 196-8. https://doi.org/10.1107/S1744309111053942

Kubiak XJP, Pluvinage B, Li de la Sierra-Gallay I, Weber P, Haouz A, Dupret J-M et al. Purification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3]. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online. 2012 feb. 1;68(Pt 2):196-8. doi: 10.1107/S1744309111053942

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title = "Purification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3]",

abstract = "Arylamine N-acetyltransferases (NATs) are xenobiotic metabolizing enzymes (XMEs) that catalyze the acetylation of arylamines. All functional NATs described to date possess a strictly conserved Cys-His-Asp catalytic triad. Here, the purification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3], a putative NAT isoenzyme that possesses a unique catalytic triad containing a glutamate residue, is reported. The crystal diffracted to 2.42 {\AA} resolution and belonged to the monoclinic space group C121, with unit-cell parameters a = 90.44, b = 44.52, c = 132.98 {\AA}, β = 103.8°.",

keywords = "Arylamine N-Acetyltransferase, Bacillus cereus, Crystallization, Crystallography, X-Ray",

author = "Kubiak, {Xavier Jean Philippe} and Benjamin Pluvinage and {Li de la Sierra-Gallay}, In{\`e}s and Patrick Weber and Ahmed Haouz and Jean-Marie Dupret and Fernando Rodrigues-Lima",

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AU - Kubiak, Xavier Jean Philippe

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AU - Li de la Sierra-Gallay, Inès

AU - Weber, Patrick

AU - Haouz, Ahmed

AU - Dupret, Jean-Marie

AU - Rodrigues-Lima, Fernando

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AB - Arylamine N-acetyltransferases (NATs) are xenobiotic metabolizing enzymes (XMEs) that catalyze the acetylation of arylamines. All functional NATs described to date possess a strictly conserved Cys-His-Asp catalytic triad. Here, the purification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3], a putative NAT isoenzyme that possesses a unique catalytic triad containing a glutamate residue, is reported. The crystal diffracted to 2.42 Å resolution and belonged to the monoclinic space group C121, with unit-cell parameters a = 90.44, b = 44.52, c = 132.98 Å, β = 103.8°.

KW - Arylamine N-Acetyltransferase

KW - Bacillus cereus

KW - Crystallization

KW - Crystallography, X-Ray

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JO - Acta Crystallographica Section F: Structural Biology Communications

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Purification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3]

Abstract

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