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Preliminary X‐ray crystallographic analysis of ornithine acetyltransferase (Rv1653) from Mycobacterium tuberculosis

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The gene product of open reading frame Rv1653 from Mycobacterium tuberculosis is annotated as encoding a probable ornithine acetyltransferase (OATase; EC 2.3.1.35), an enzyme that catalyzes two steps in the arginine‐biosynthesis pathway. It transfers an acetyl group from N‐acetylornithine to l‐glutamate to produce N‐acetylglutamate and l‐ornithine. Rv1653 was crystallized using the sitting‐drop vapour‐diffusion method. The native crystals diffracted to a resolution of 1.7 Å and belonged to space group P212121, with unit‐cell parameters a = 60.1, b = 99.7, c = 155.3 Å. The preliminary X‐ray study showed the presence of a dimer in the asymmetric unit of the crystals, which had a Matthews coefficient V M of 2.8 Å3 Da−1.
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Keywords: Mycobacterium tuberculosis; N‐terminal nucleophiles; arginine biosynthesis; ornithine acetyltransferase

Document Type: Research Article

Affiliations: Protein Structure and Function Group, Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

Publication date: February 1, 2009

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