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Preliminary X-ray Diffraction Analysis of Purine Nucleoside Phosphorylase from the Haloalkaliphilic Bacterium Halomonas chromatireducens
- Authors: Safonova T.N.1, Antipov A.N.1, Veiko V.P.1, Mordkovich N.N.1,2, Okorokova NA.1, Dorovatovskii P.V.3, Polyakov K.M.4
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Affiliations:
- 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
- National Research Centre “Kurchatov Institute”, 123098, Moscow, Russia
- Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991, Moscow, Russia
- Issue: Vol 68, No 6 (2023)
- Pages: 922-925
- Section: STRUCTURE OF MACROMOLECULAR COMPOUNDS
- URL: https://rjmseer.com/0023-4761/article/view/673289
- DOI: https://doi.org/10.31857/S0023476123600301
- EDN: https://elibrary.ru/XSCQXA
- ID: 673289
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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
- 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
- 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
- Krenitsky T.A., Koszalka G.W., Tuttle J.V. // Biochemistry. 1981. V. 20 (12). P. 3615. https://doi.org/10.1021/bi00515a048
- 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
- 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
- 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
- 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
- Xie X., Xia J., He K. et al. // Biotechnol. Lett. 2011. V. 33. P. 1107. https://doi.org/10.1007/s10529-011-0535-6
- 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
- Carmeliet P. // Nature. 2005. V. 438. № 7070. P. 932. https://doi.org/10.1038/nature04478
- 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
- Pant P., Pathak A., Jayaram B. // J. Phys. Chem. B. 2021. V. 125. P. 2856. https://doi.org/10.1021/acs.jpcb.0c10553
- 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
- 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
- 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
- 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
- Шаповалова А.А., Хижняк Т.В., Турова Т.П. и др. // Микробиология. 2009. Т. 78. № 1. С. 117. https://doi.org/10.1134/S0026261709010135
- Мордкович Н.Н., Манувера В.А., Вейко В.П. и др. // Биотехнология. 2012. № 1. С. 21.
- Kabsch W. // Acta. Cryst. D. 2010. V. 66. P. 125. https://doi.org/10.1107/S0907444909047337
- 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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