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Three-dimensional structure of phosphoribosyl pyrophosphate synthetase from E. coli at 2.71 Å resolution

Abstract

Phosphoribosyl pyrophosphate synthetase from Escherichia coli was cloned, purified, and crystallized. Single crystals of the enzyme were grown under microgravity. The X-ray diffraction data set was collected at the Spring-8 synchrotron facility and used to determine the three-dimensional structure of the enzyme by the molecular-replacement method at 2.71 Å resolution. The active and regulatory sites in the molecule of E. coli phosphoribosyl pyrophosphate synthetase were revealed by comparison with the homologous protein from Bacillus subtilis, the structure of which was determined in a complex with functional ligands. The conformations of polypeptide-chain fragments surrounding and composing the active and regulatory sites were shown to be identical in both proteins.

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Correspondence to V. I. Timofeev.

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Original Russian Text © V.I. Timofeev, Yu.A. Abramchik, N.E. Zhukhlistova, T.I. Muravieva, R.S. Esipov, I.P. Kuranova, 2016, published in Kristallografiya, 2016, Vol. 61, No. 1, pp. 51–61.

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Timofeev, V.I., Abramchik, Y.A., Zhukhlistova, N.E. et al. Three-dimensional structure of phosphoribosyl pyrophosphate synthetase from E. coli at 2.71 Å resolution. Crystallogr. Rep. 61, 44–54 (2016). https://doi.org/10.1134/S1063774516010247

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  • DOI: https://doi.org/10.1134/S1063774516010247

Keywords

  • Crystallography Report
  • Allosteric Site
  • Flexible Loop
  • Phosphoribosyl Pyrophosphate
  • Invariant Residue