Open AccessPurification, crystallization and preliminary X‐ray characterization of Bacillus cereus arylamine N ‐acetyltransferase 3 [(BACCR)NAT3]
Author(s) -
Kubiak Xavier,
Pluvinage Benjamin,
Li de la SierraGallay Inès,
Weber Patrick,
Haouz Ahmed,
Dupret JeanMarie,
RodriguesLima Fernando
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111053942
Subject(s) - bacillus cereus , crystallization , characterization (materials science) , chemistry , nuclear chemistry , crystallography , materials science , organic chemistry , biology , bacteria , nanotechnology , genetics
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 C 121, with unit‐cell parameters a = 90.44, b = 44.52, c = 132.98 Å, β = 103.8°.