Purification, crystallization and preliminary X-ray characterization ofBacillus cereusarylamineN-acetyltransferase 3 [(BACCR)NAT3] - Archive ouverte HAL Access content directly
Journal Articles Acta Crystallographica Section F: Structural Biology and Crystallization Communications Year : 2012

Purification, crystallization and preliminary X-ray characterization ofBacillus cereusarylamineN-acetyltransferase 3 [(BACCR)NAT3]

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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 Å resolution and belonged to the monoclinic space group C121, with unit-cell parameters a = 90.44, b = 44.52, c = 132.98 Å , = 103.8 .

Dates and versions

pasteur-03525338 , version 1 (13-01-2022)

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Xavier Kubiak, Benjamin Pluvinage, Inès Li de La Sierra-Gallay, Patrick Weber, Ahmed Haouz, et al.. Purification, crystallization and preliminary X-ray characterization ofBacillus cereusarylamineN-acetyltransferase 3 [(BACCR)NAT3]. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2012, 68 (2), pp.196 - 198. ⟨10.1107/s1744309111053942⟩. ⟨pasteur-03525338⟩
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