EXTRACTION, PURIFICATION, AND SMALL-ANGLE X-RAY SCATTERING ANALYSIS OF THE YSXC GTPASE OF STAPHYLOCOCCUS AUREUS

Мұқаба

Дәйексөз келтіру

Толық мәтін

Ашық рұқсат Ашық рұқсат
Рұқсат жабық Рұқсат берілді
Рұқсат жабық Тек жазылушылар үшін

Аннотация

Study of the structures of various biological macromolecules is one of the main directions that are intensively developed using physical methods. Since proteins are an elementary unit of the structural and functional organization of a cell, the strategies for combating pathogenic microorganisms include the analysis of the bacterial protein synthesis apparatus and related systems. The extraction, purification, and small-angle X-ray scattering analysis of the structure of YsxC protein from the Staphylococcus aureus pathogenic bacterium are reported. This protein is involved in the cell growth and division processes, serves an energy-dependent factor, and participates in the assembly of large ribosome subunit. The structural study of this protein opens up a possibility of searching for small molecules capable of inhibiting its function. Since the structural variability of protein factors is higher than that of the conservative ribosome sites, their inhibition makes it possible to selectively affect a pathogenic microorganism.

Авторлар туралы

A. Biktimirov

Kazan (Volga Region) Federal University, Kazan, 420008 Russia

Email: k.usachev@kpfu.ru
Россия, Казань

D. Islamov

Kazan (Volga Region) Federal University, Kazan, 420008 Russia

Email: k.usachev@kpfu.ru
Россия, Казань

S. Validov

Kazan (Volga Region) Federal University, Kazan, 420008 Russia

Email: k.usachev@kpfu.ru
Россия, Казань

G. Peter's

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

Email: k.usachev@kpfu.ru
Россия, Москва

A. Khaliullina

Kazan (Volga Region) Federal University, Kazan, 420008 Russia

Email: k.usachev@kpfu.ru
Россия, Казань

M. Yusupov

Institut de génétique et de biologie moléculaire et cellulaire, 67400 Illkirch-Graffenstaden, France

Email: k.usachev@kpfu.ru
Франция, Илькирш-Граффенштаден

K. Usachev

Kazan (Volga Region) Federal University, Kazan, 420008 Russia

Хат алмасуға жауапты Автор.
Email: k.usachev@kpfu.ru
Россия, Казань

Әдебиет тізімі

  1. Chambers H.F., Deleo F.R. // Nat Rev Microbiol. 2009. V. 7 № 9. P. 629. https://doi.org/10.1038/nrmicro2200
  2. Stapleton P.D., Taylor P.W. // Sci Prog. 2002. V. 85 № 1. P. 57. https://doi.org/10.3184/003685002783238870
  3. Gan T., Shu G., Fu H. et al. // BMC Vet Res. 2021. V. 17 P. 177. https://doi.org/10.1186/s12917-021-02884-z
  4. Murray Ch.J.L., Shunji I.K., Sharara F. et al. // Lancet. 2022. V. 10325. № 399. P. 629. https://doi.org/10.1016/S0140-6736(21)02724-0
  5. Poehlsgaard J., Douthwaite S. // Nat. Rev. Microbiol. 2005. V. 3. P. 870. https://doi.org/10.1038/nrmicro1265
  6. Усачев К.С., Юсупов М.М., Валидов Ш.З. // Биохимия. 2020. Т. 85. № 11. С. 1690. https://doi.org/10.1134/S0006297920110115
  7. Khusainov I., Fatkhullin B., Pellegrino S. // Nature Commun. 2020. V. 11 № 1656. https://doi.org/10.1038/s41467-020-15517-0
  8. Cooper E.L., García-Lara J., Foster S.J. // BMC Microbiol. 2009. V. 9. № 266. https://doi.org/10.1186/1471-2180-9-266
  9. Ramakrishnan C., Dani V.S., Ramasarma T. // Protein Eng. Des. Sel. 2002. V. 15. № 10. P. 783. https://doi.org/10.1093/protein/15.10.783
  10. Ni X., Davis J.H., Jain N. et al. // Nucl. Acids Res. 2016. V. 44. № 17. P. 8442. https://doi.org/10.1093/nar/gkw678
  11. Корчуганов В.Н., Валентинов А.Г., Полозов С.М. и др. // Кристаллография. 2022. Т. 67. № 5. С. 735. https://doi.org/10.31857/S0023476122050058
  12. Konarev P.V., Volkov V.V., Sokolova A.V. et al. // J. Appl. Cryst. 2003. V. 36. P. 1277. https://doi.org/10.1107/S0021889803012779
  13. Svergun D.I. // Biophys J. 1999. V. 76. № 6. P. 2879. https://doi.org/10.1016/S0006-3495(99)77443-6
  14. Gosavi R.A., Mueser T.C., Schall C.A. // Acta Cryst. 2008. V. 64. P. 506. https://doi.org/10.1107/S0907444908004265
  15. Ruzheinikov S.N., Das Sanjan K., Sedelnikova S.E. et al. // J. Mol. Biol. 2004. V. 339 № 2. P. 265. https://doi.org/10.1016/j.jmb.2004.03.043
  16. Goldenberg D.P., Argyle B. // Biophys. J. 2014. V. 106. № 4. P. 895. https://doi.org/10.1016/j.bpj.2013.12.004
  17. Chacon P., Moran F., Dia z J.F. et al. // Biophys. J. 1998. V. 74. P. 2760. https://doi.org/10.1016/S0006-3495(98)77984-6
  18. Svergun D.I., Barberato C., Koch M.H.J. // J. Appl. Cryst. 1999. V. 28. P. 768. https://doi.org/10.1107/S1600576717007786
  19. Jumper J., Evans R., Pritzel A. et al. // Nature. 2021. V. 596. P. 583. https://doi.org/10.1038/s41586-021-03819-2

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© А.Д. Биктимиров, Д.Р. Исламов, Ш.З. Валидов, Г.С. Петерс, А.В. Халиуллина, М.М. Юсупов, К.С. Усачев, 2023

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