- PII
- 10.31857/S0023476123010137-1
- DOI
- 10.31857/S0023476123010137
- Publication type
- Status
- Published
- Authors
- Volume/ Edition
- Volume 68 / Issue number 2
- Pages
- 276-280
- Abstract
- Protein crystal structure studies are an important tool for drug design. The growth of high-quality crystals suitable for X-ray diffraction is the limiting factor and the bottleneck in obtaining the structural data. Here we report the extraction, purification, and crystallization of the protein GTPase Era from the pathogenic bacterium Staphylococcus aureus. In bacterial cells, GTPase Era acts as a ribosome assembly factor. This enzyme is responsible for the cell growth and division. However, its structure is poorly understood. We obtained crystals of Staphylococcus aureus GTPase Era, which can be used in further structural studies by single-crystal X-ray diffraction analysis.
- Keywords
- PROTEIN CRYSTAL STRUCTURE X-RAY DIFFRACTION
- Date of publication
- 15.09.2025
- Year of publication
- 2025
- Number of purchasers
- 0
- Views
- 13
References
- 1. Stijn Blot R.N., Vandewoude K., Colardyn F. // N. Engl. J. Med. 1998. V. 339 (27). P. 2025. https://doi.org/10.1056/nejm199812313392716
- 2. Jeljaszewicz J., Mlynarczyk G., Mlynarczyk A. // Int. J. Antimicrob. Agents. 2000. V. 16 (4). P. 473. https://doi.org/10.1016/S0924-8579 (00)00289-2
- 3. Fierobe L., Decré D., Mùller C. et al. // Clin. Infect. Dis. 1999. V. 29 (5). P. 1231. https://doi.org/10.1086/313454
- 4. Shajani Z., Sykes M.T., Williamson J.R. // Annu. Rev. Biochem. 2011. V. 80. P. 501. https://doi.org/10.1146/annurev-biochem-062608-160432
- 5. Kaczanowska M., Rydén-Aulin M. // Microbiol. Mol. Biol. Rev. 2007. V. 71 (3). P. 477. https://doi.org/10.1128/MMBR.00013-07
- 6. Усачев К.С., Юсупов М.М., Валидов Ш.З. // Биохимия. 2020. Т. 85 (11). С. 1690. https://doi.org/10.1134/S0006297920110115
- 7. Stern S., Powers T., Changchien L.I.-M., Noller H.F. // Science. 1989. V. 244 (4906). P. 783. https://doi.org/10.1126/science.2658053
- 8. Davis J.H., Williamson J.R. // Philos. Trans. R. Soc. 2017. V. 372 (1716). Art. 20160181. https://doi.org/10.1098/rstb.2016.0181
- 9. Bourne H.R. // Philos. Trans. R. Soc. 1995. V. 349 (1329). P. 283. https://doi.org/10.1098/rstb.1995.0114
- 10. Tu C., Zhou X., Tropea J. et al. // Proc. Natl. Acad. Sci. U S A. 2009. V. 106 (35). P. 14843. https://doi.org/10.1073/pnas.0904032106
- 11. Simon Goto, Akira Muto, Hyouta Himeno // J. Biochem. 2013. V. 153 (5). P. 403. https://doi.org/10.1093/jb/mvt022
- 12. Ji X. // Postepy Biochem. 2016. V. 62 (3). P. 335.
- 13. Xiaomei Zhou, Howard K. Peters III, Xintian Li et al. // J. Bacteriol. 2020. V. 202. P. 21. https://doi.org/10.1128/JB.00342-20
- 14. Ren H., Liang Y., Li R. et al. // Acta Cryst. D. 2004. V. 60. P. 1292. https://doi.org/10.1107/S0907444904010467
- 15. Meulenbroek E., Pannu N. // Acta Cryst. F. 2011. V. 68. P. 45. https://doi.org/10.1107/S1744309111045842
- 16. Murugova T.N., Vlasov A.V., Ivankov O.I. et al. // J. Optoelectron. Adv. Mater. 2015. V. 17. P. 1397.
- 17. Kabsch W. // Xds. Acta Cryst. D. 2010. V. 66. P. 125. https://doi.org/10.1107/S0907444909047337
- 18. Chen X., Chen S.-M., Powell B. et al. // FEBS Lett. 1999. V. 445. P. 425. https://doi.org/10.1016/S0014-5793 (99)00178-7
- 19. Manalastas-Cantos K., Konarev P.V., Hajizadeh N.R. et al. // J. Appl. Cryst. 2021. V. 54. P. 343. https://doi.org/10.1107/S1600576720013412
- 20. Jumper J., Evans R., Pritzel A. et al. // Nature. 2021. V. 596 (7873). P. 583.
- 21. Chen X., Court D.L., Ji X. // PNAS. 1999. V. 15 (96). P. 8396. https://doi.org/10.1073/pnas.96.15.8396
