Preliminary X-ray Diffraction Analysis of Purine Nucleoside Phosphorylase from the Haloalkaliphilic Bacterium Halomonas chromatireducens

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Abstract

Crystals of the enzyme purine nucleoside phosphorylase from the extremophilic bacterium Halomonas Chromatireducens AGD 8-3, suitable for X-ray diffraction, were grown by the vapor-diffusion method. The X-ray diffraction data were collected from these crystals at the Belok beamline of the Kurchatov synchrotron radiation source (National Research Centre “Kurchatov Institute”) at 100 K to 1.80 Å resolution. The X-ray diffraction data were processed in the space groups P1, P2, P21, and P622. The structure was solved by the molecular replacement method taking into account the twinning in the space groups P21 and P1 with one and two hexamers of the enzyme per asymmetric unit, respectively.

About the authors

T. N. Safonova

Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology,” Russian Academy of Sciences, 119071, Moscow, Russia

Email: tn_safonova@mail.ru
Россия, Москва

A. N. Antipov

Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology,” Russian Academy of Sciences, 119071, Moscow, Russia

Email: kmpolyakov@gmail.com
Россия, Москва

V. P. Veiko

Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology,” Russian Academy of Sciences, 119071, Moscow, Russia

Email: kmpolyakov@gmail.com
Россия, Москва

N. N. Mordkovich

Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology,” Russian Academy of Sciences, 119071, Moscow, Russia; Bochkov Research Centre for Medical Genetics, 115522, Moscow, Russia

Email: kmpolyakov@gmail.com
Россия, Москва; Россия, Москва

N A. Okorokova

Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology,” Russian Academy of Sciences, 119071, Moscow, Russia

Email: kmpolyakov@gmail.com
Россия, Москва

P. V. Dorovatovskii

National Research Centre “Kurchatov Institute”, 123098, Moscow, Russia

Email: kmpolyakov@gmail.com
Россия, Москва

K. M. Polyakov

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991, Moscow, Russia

Author for correspondence.
Email: kmpolyakov@gmail.com
Россия, Москва

References

  1. Ealick S.E., Rule S.A., Carter D.C. et al. // J. Biol. Chem. 1990. V. 265. P. 1812. https://doi.org/10.1016/S0021-9258(19)40090-2
  2. Mao C., Cook W.J., Zhou M. et al. // Structure. 1997. V. 5. P. 1373. https://doi.org/10.1016/S0969-2126(97)00287-6
  3. Krenitsky T.A., Koszalka G.W., Tuttle J.V. // Biochemistry. 1981. V. 20 (12). P. 3615. https://doi.org/10.1021/bi00515a048
  4. Bennett E.M., Li C., Allan P.W. et al. // J. Biol. Chem. 2003. V. 278. P. 47110. https://doi.org/10.1074/jbc.M304622200
  5. Ducati R.G., Santos D.S., Basso L.A. // Arch. Biochem. Biophys. 2009. V. 486. P. 155. https://doi.org/10.1016/j.abb.2009.04.011
  6. Михайлопуло И.А., Мирошников А.И. // Acta Naturae. 2010. Т. 2. № 2. С. 36. https://doi.org/10.32607/20758251-2010-2-2-36-58
  7. Nannemann D.P., Kaufmann K.W., Meiler J. et al. // Protein Eng. Des. Sel. 2010. V. 23. P. 607. https://doi.org/10.1093/protein/gzq033
  8. Xie X., Xia J., He K. et al. // Biotechnol. Lett. 2011. V. 33. P. 1107. https://doi.org/10.1007/s10529-011-0535-6
  9. Liekens S., De Clercq E., Neyts J. // Biochem. Pharmacol. 2001. V. 61. № 3. P. 253. https://doi.org/10.1016/s0006-2952(00)00529-3
  10. Carmeliet P. // Nature. 2005. V. 438. № 7070. P. 932. https://doi.org/10.1038/nature04478
  11. Furukawa T., Tabata S., Yamamoto M. et al. // Pharmacol. Res. 2018. V. 132. P. 15 https://doi.org/10.1016/j.phrs.2018.03.019
  12. Pant P., Pathak A., Jayaram B. // J. Phys. Chem. B. 2021. V. 125. P. 2856. https://doi.org/10.1021/acs.jpcb.0c10553
  13. Madrid D.C., Ting L.-M., Waller K.L. et al. // J. Biol. Chem. 2008. V. 283. P. 35899. https://doi.org/10.1074/jbc.M807218200
  14. Myers L.A., Hershfield M.S., Neale W.T. et al. // J. Pediatr. 2004. V. 145. P. 710. https://doi.org/10.1016/j.jpeds.2004.06.075
  15. Погосян Л.Г., Нерсесова Л.С., Газарянц М.Г. и др. // Биомед. химия. 2011. Т. 57. № 5. С. 526. https://doi.org/10.18097/PBMC20115705526
  16. Антипов А.Н., Мордкович Н.Н., Хижняк Т.В. и др. // Прикл. биохим. микробиол. 2020. Т. 56. № 1. С. 45. https://doi.org/10.31857/S055510992001002X
  17. Шаповалова А.А., Хижняк Т.В., Турова Т.П. и др. // Микробиология. 2009. Т. 78. № 1. С. 117. https://doi.org/10.1134/S0026261709010135
  18. Мордкович Н.Н., Манувера В.А., Вейко В.П. и др. // Биотехнология. 2012. № 1. С. 21.
  19. Kabsch W. // Acta. Cryst. D. 2010. V. 66. P. 125. https://doi.org/10.1107/S0907444909047337
  20. Murshudov G.N., Skubák P., Lebedev A.A. et al. // Acta Cryst. D. 2011. V. 67. P. 355. https://doi.org/10.1107/S0907444911001314

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