Crystallization and preliminary X-ray characterization of arylamine N-acetyltransferase C (BanatC) from Bacillus anthracis

Journal Article · Mon Oct 01 00:00:00 EDT 2007 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309107041814· OSTI ID:22360405

Pluvinage, Benjamin ^[1]; Martins, Marta; Ragunathan, Nilusha ^[1]; Dupret, Jean-Marie; Rodrigues-Lima, Fernando ^[1]

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1. Laboratoire de Cytophysiologie et Toxicologie Cellulaire (EA 1553), Université Paris Diderot-Paris 7, 75005 Paris (France)

Bacillus anthracis arylamine N-acetyltransferase C (BanatC) is an enzyme that metabolizes the drug sulfamethoxazole. Crystals of the purified enzyme that diffract at 1.95 Å are reported. The arylamine N-acetyltransferase (NAT) enzymes are xenobiotic metabolizing enzymes that have been found in a large range of eukaryotes and prokaryotes. These enzymes catalyse the acetylation of arylamine drugs and/or pollutants. Recently, a Bacillus anthracis NAT isoform (BanatC) has been cloned and shown to acetylate the sulfonamide antimicrobial sulfamethoxazole (SMX). Subsequently, it was shown that BanatC contributes to the resistance of this bacterium to SMX. Here, the crystallization and the X-ray characterization of BanatC (Y38F mutant) are reported. The crystals belong to the tetragonal space group P4{sub 1}2{sub 1}2 or P4{sub 3}2{sub 1}2, with unit-cell parameters a = b = 53.70, c = 172.40 Å, and diffract to 1.95 Å resolution on a synchrotron source.

• OSTI ID: 22360405
• Journal Information: Acta Crystallographica. Section F, Vol. 63, Issue Pt 10; Other Information: PMCID: PMC2339728; PMID: 17909290; PUBLISHER-ID: ll5126; OAI: oai:pubmedcentral.nih.gov:2339728; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
CRYSTALS
RESOLUTION
SPACE GROUPS