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Crystallization and preliminary X-ray diffraction study of phosphopantetheine adenylyltransferase from M. tuberculosis crystallizing in space group P32

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Abstract

Crystals of M. tuberculosis phosphopantetheine adenylyltransferase were grown in microgravity by the capillary counter-diffusion method through a gel layer. The X-ray diffraction data set suitable for the determination of the three-dimensional structure at atomic resolution was collected from one crystal at the Spring-8 synchrotron facility to 2.00-Å resolution. The crystals belong to sp. gr. P32 and have the following unit-cell parameters: a = b = 106.47 Å, c = 71.32 Å, α = γ = 90°, β = 120°. The structure was solved by the molecular-replacement method. There are six subunits of the enzyme comprising a hexamer per asymmetric unit. The hexamer is a biologically active form of phosphopantetheine adenylyltransferase from M. tuberculosis.

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Authors and Affiliations

  1. Shubnikov Institute of Crystallography, Russian Academy of Sciences, Leninskii pr. 59, Moscow, 119333, Russia

    V. I. Timofeev & I. P. Kuranova

  2. Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117997, Russia

    L. A. Chupova & R. S. Esipov

  3. National Research Centre “Kurchatov Institute,”, pl. Akademika Kurchatova 1, Moscow, 123098, Russia

    V. I. Timofeev & I. P. Kuranova

Authors
  1. V. I. Timofeev
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  2. L. A. Chupova
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  3. R. S. Esipov
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  4. I. P. Kuranova
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Correspondence to V. I. Timofeev.

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Original Russian Text © V.I. Timofeev, L.A. Chupova, R.S. Esipov, I.P. Kuranova, 2015, published in Kristallografiya, 2015, Vol. 60, No. 5, pp. 745–747.

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Timofeev, V.I., Chupova, L.A., Esipov, R.S. et al. Crystallization and preliminary X-ray diffraction study of phosphopantetheine adenylyltransferase from M. tuberculosis crystallizing in space group P32 . Crystallogr. Rep. 60, 682–684 (2015). https://doi.org/10.1134/S106377451505017X

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  • DOI: https://doi.org/10.1134/S106377451505017X

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