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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1274-7. doi: 10.1107/S1744309111028958. Epub 2011 Sep 30.

Cloning, expression, purification, crystallization and preliminary X-ray studies of the C-terminal domain of Rv3262 (FbiB) from Mycobacterium tuberculosis.

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Structural Biology Laboratory, School of Biological Sciences, The University of Auckland, Auckland, New Zealand.


During cofactor F(420) biosynthesis, the enzyme F(420)-γ-glutamyl ligase (FbiB) catalyzes the addition of γ-linked L-glutamate residues to form polyglutamylated F(420) derivatives. In Mycobacterium tuberculosis, Rv3262 (FbiB) consists of two domains: an N-terminal domain from the F(420) ligase superfamily and a C-terminal domain with sequence similarity to nitro-FMN reductase superfamily proteins. To characterize the role of the C-terminal domain of FbiB in polyglutamyl ligation, it has been purified and crystallized in an apo form. The crystals diffracted to 2.0 Å resolution using a synchrotron source and belonged to the tetragonal space group P4(1)2(1)2 (or P4(3)2(1)2), with unit-cell parameters a = b = 136.6, c = 101.7 Å, α = β = γ = 90°.

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