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

Department of Neuroscience

5 Citations (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°.

Original language	English
Journal	Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online
Volume	68
Issue number	Pt 2
Pages (from-to)	196-8
Number of pages	3
ISSN	1744-3091
DOIs	https://doi.org/10.1107/S1744309111053942
Publication status	Published - 1 Feb 2012

Keywords

Arylamine N-Acetyltransferase
Bacillus cereus
Crystallization
Crystallography, X-Ray

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10.1107/S1744309111053942

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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.

In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, Vol. 68, No. Pt 2, 01.02.2012, p. 196-8.

Research output: Contribution to journal › Journal article › Research › 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, vol. 68, no. Pt 2, pp. 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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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°.",

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AU - Weber, Patrick

AU - Haouz, Ahmed

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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

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KW - Crystallography, X-Ray

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

Abstract

Keywords

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