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© Ahmed Haouz
Cristaux d'une protéine de Mycobacterium tuberculosis produits dans le cadre du Grand Programme Horizontal sur la Tuberculose à l'Institut Pasteur. La caractérisation structurale de protéines mycobactériennes aide à une meilleure compréhension de la physiologie et de la pathogénicité des mycobactéries et fournit un point de départ pour la conception de nouveaux agents antibactériens.
Publication : Acta crystallographica. Section F, Structural biology and crystallization communications

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section F, Structural biology and crystallization communications - 26 Jan 2012

Kubiak X, Pluvinage B, Li de la Sierra-Gallay I, Weber P, Haouz A, Dupret JM, Rodrigues-Lima F

Link to Pubmed [PMID] – 22297998

Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2012 Feb;68(Pt 2):196-8

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°.

http://www.ncbi.nlm.nih.gov/pubmed/22297998