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. 2013 Dec;69(Pt 12):1354-6.
doi: 10.1107/S1744309113027000. Epub 2013 Nov 28.

Purification, crystallization and preliminary X-ray studies of MbtN (Rv1346) from Mycobacterium tuberculosis

Ai Fen Chai  1 , Jodie M Johnston, Richard D Bunker, Esther M M Bulloch, Genevieve L Evans, J Shaun Lott, Edward N Baker
Affiliations

Purification, crystallization and preliminary X-ray studies of MbtN (Rv1346) from Mycobacterium tuberculosis

Ai Fen Chai et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec.

Abstract

In Mycobacterium tuberculosis, the protein MbtN (Rv1346) catalyzes the formation of a double bond in the fatty-acyl moiety of the siderophore mycobactin, which is used by this organism to acquire essential iron. MbtN is homologous to acyl-CoA dehydrogenases, whose general role is to catalyze the α,β-dehydrogenation of fatty-acyl-CoA conjugates. Mycobactins, however, contain a long unsaturated fatty-acid chain with an unusual cis double bond conjugated to the carbonyl group of the mycobactin core. To characterize the role of MbtN in the dehydrogenation of this fatty-acyl moiety, the enzyme has been expressed, purified and crystallized. The crystals diffracted to 2.3 Å resolution at a synchrotron source and were found to belong to the hexagonal space group H32, with unit-cell parameters a = b = 139.10, c = 253.09 Å, α = β = 90, γ = 120°.

Keywords: MbtN; Mycobacterium tuberculosis; Rv1346.

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Figures

Figure 1
Figure 1
Crystals of MbtN shown under polarized light.
Figure 2
Figure 2
A typical diffraction image obtained from the MbtN crystals.
See this image and copyright information in PMC

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