Effect of Microgravity on the Crystallization of Cardiotoxin from the Venom of Spectacled Cobra Naja naja

K. M. Dubova; Дубова К. М.; P. V. Dubovskii; Дубовский П. В.; Yu. N. Utkin; Уткин Ю. Н.; V. R. Samygina; Самыгина В. Р.

doi:10.31857/S0023476123600465

Effect of Microgravity on the Crystallization of Cardiotoxin from the Venom of Spectacled Cobra Naja naja

作者: Dubova K.M.¹^,2, Dubovskii P.V.³, Utkin Y.N.³, Samygina V.R.¹^,2
隶属关系:
1. National Research Centre “Kurchatov Institute”, 123182, Moscow, Russia
2. Shubnikov Institute of Crystallography, Federal Scientific Research Centre “Crystallography and Photonics,” Russian Academy of Sciences, 119333, Moscow, Russia
3. Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997, Moscow, Russia
期: 卷 68, 编号 6 (2023)
页面: 902-906
栏目: STRUCTURE OF MACROMOLECULAR COMPOUNDS
URL: https://rjmseer.com/0023-4761/article/view/673281
DOI: https://doi.org/10.31857/S0023476123600465
EDN: https://elibrary.ru/HZBNYG
ID: 673281

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详细

Cardiotoxins, which belong to the family of three-finger toxins, are the main components of cobra venom. They exhibit various types of biological activity, including antimicrobial and cytotoxic against cancer cells. Data on the minimal structural differences between individual toxins are necessary for understanding the molecular mechanisms of their action. This information can be obtained by high-resolution X-ray diffraction analysis. The influence of microgravity on the crystal packing and diffraction quality of crystals of cardiotoxin from cobra Naja naja has been investigated. Cardiotoxin crystals, which were grown on the International Space Station, provided maximally high resolution for the structure of this toxin. Protein crystallized extremely in the hexagonal space group, whereas more than half of crystals grown under laboratory conditions belonged to the orthorhombic system.

参考

Khalil A., Elesawy B.H., Ali T.M. et al. // Molecules. 2021. V. 26. P. 4941. https://doi.org/10.3390/molecules26164941
Dubovskii P.V., Efremov R.G. // Expert Rev. Proteomics. 2018. V. 15. P. 873. https://doi.org/10.1080/14789450.2018.1537786
Kalita B., Utkin Y.N., Mukherjee A.K. // Toxins (Basel). 2022. V. 14. P. 839. https://doi.org/10.3390/toxins14120839
Joubert F.J. // Eur. J. Biochem. 1977. V. 74. P. 387. https://doi.org/10.1111/j.1432-1033.1977.tb11403.x
Gayatri S., Gorai B., Sivaraman T. // Res. J. Pharm. Biol. Chem. Sci. 2016. V. 7. P. 936.
Konshina A.G., Dubovskii P.V., Efremov R.G. // Curr. Protein Pept. Sci. 2012. V. 13 (6). P. 570.
Дубовский П.В., Уткин Ю.Н. // Acta Naturae. 2014. Т. 6. № 3. С. 12.
Chien K.Y., Chiang C.M., Hseu Y.C. // J. Biol. Chem. 1994. V. 269. P. 14473.
Dubovskii P.V., Ignatova A.A., Alekseeva A.S. // Toxins. 2022. V. 15. P. 6. https://doi.org/10.3390/toxins15010006
Dubovskii P.V., Dubova K.M., Bourenkov G. et al. // Toxins. 2022. V. 14. P. 149. https://doi.org/10.3390/toxins14020149
Luna A., Meisel J., Hsu K. et al. // NPJ Microgravity. 2020. V. 6. P. 12. https://doi.org/10.1038/s41526-020-0102-3
Shabalin I.G., Serov A.E., Skirgello O.E. et al. // Crystallography Reports. 2010. V. 55 P. 806. https://doi.org/10.1134/S1063774510050159
Timofeev V., Samygina V. // Crystals. 2022. V. 13. P. 71. https://doi.org/10.3390/cryst13010071
Esposito L., Sica F., Sorrentino G. et al. // Acta Cryst. D. 1998. V. 54. P. 386. https://doi.org/10.1107/s0907444997011992
Dubova K.M., Sokolov A.V., Gorbunov N.P. et al. // Crystallography Reports. 2018. V. 63. P. 951. https://doi.org/10.1134/S1063774518060111
Tanaka H., Inaka K., Sughiyama Sh. // J. Synchrotron Rad. 2004. V. 11. P. 45. https://doi.org/10.1107/S0909049503023446
Takahashi S., Tsurumura T., Aritake K. et al. // Acta Cryst. F. 2010. V. 66. P. 846. https://doi.org/10.1107/S1744309110020828
Boyko K.M., Timofeev V.I., Samygina V.R. et al. // Crystallography Reports. 2016. V. 61. № 5. P. 718. https://doi.org/10.1134/S1063774516050059
Kabsch W. // Acta Cryst. D. 2010. V. 66. P. 133. https://doi.org/10.1107/S0907444909047374
Evans P.R., Murshudov G.N. // Acta Cryst. D. 2013. V. 69. P. 1204. https://doi.org/10.1107/S0907444913000061
Agirre J., Atanasova M., Bagdonas H. et al. // Acta. Cryst. D. 2023. V. 79. P. 449. https://doi.org/10.1107/ S2059798323003595
Schrödinger L., DeLano W. 2020. PyMOL. http://www.pymol.org/pymol
Chruszcz M., Potrzebowski W., Zimmerman M.D. et al. // Protein Sci. 2008. V. 17. P. 623. http://www.proteinscience.org/cgi/doi/ 10.1110/ps.073360508
Shabalin I.G., Tikhonova T.V., Polyakov K.M. et al. // EMBL Annual. 2007. Rep. 2. P. 109.
Eistrikh-Heller P.A., Rubinsky S.V., Samygina V.R. et al. // Crystallography Reports. 2021. V. 66. P. 777. https://doi.org/10.1134/S1063774521050059
Inaka K., Takahashi S., Aritake K. et al. // Cryst. Growth Des. 2011. V. 11. P. 2107. https://doi.org/10.1021/cg101370v
Rahman R.N., Ali M.S., Leow T.C. et al. // Gravitational and Space Biology. 2010. V. 23. P. 89.