Mutational and structural study of RipA, a key enzyme in Mycobacterium tuberculosis cell division: Evidence for the l-to-d inversion of configuration of the catalytic cysteine

Acta Crystallographica Section D: Biological Crystallography

Volumn 70, Issue 9, 2014, Pages 2295-2300

  Squeglia, Flavia ^a   Ruggiero, Alessia ^a   Romano, Maria ^a,b   Vitagliano, Luigi ^a   Berisio, Rita ^a  

^a CNR   (Italy)

^b SECOND UNIVERSITY OF NAPLES   (Italy)

Author keywords

cysteine protease; Mycobacterium tuberculosis; RipA

Indexed keywords

BACTERIAL PROTEIN; CYTOSINE; PRIMER DNA;

BIOCATALYSIS; CELL DIVISION; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; CYTOLOGY; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR CLONING; MUTATION; MYCOBACTERIUM TUBERCULOSIS; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PROTEIN CONFORMATION;

BACTERIAL PROTEINS; BASE SEQUENCE; BIOCATALYSIS; CELL DIVISION; CIRCULAR DICHROISM; CLONING, MOLECULAR; CYTOSINE; DNA PRIMERS; MODELS, MOLECULAR; MUTATION; MYCOBACTERIUM TUBERCULOSIS; POLYMERASE CHAIN REACTION; PROTEIN CONFORMATION;

EID: 84907016009     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S1399004714013674     Document Type: Article

References (34)

1. Amano, M., Hasegawa, J., Kobayashi, N., Kishi, N., Nakazawa, T., Uchiyama, S. & Fukui, K. (2011). Anal. Chem. 83, 3857-3864.
2. Böth, D., Schneider, G. & Schnell, R. (2011). J. Mol. Biol. 413, 247-260.
3. Buczek, O., Yoshikami, D., Bulaj, G., Jimenez, E. C. & Olivera, B. M. (2005). J. Biol. Chem. 280, 4247-4253.
4. Chao, M. C., Kieser, K. J., Minami, S., Mavrici, D., Aldridge, B. B., Fortune, S. M., Alber, T. & Rubin, E. J. (2013). PLoS Pathog. 9, e1003197.
5. Cloos, P. A. & Christgau, S. (2002). Matrix Biol. 21, 39-52.
6. Correale, S., Ruggiero, A., Capparelli, R., Pedone, E. & Berisio, R. (2013). Acta Cryst. D69, 1697-1706.
7. Goldenberg, O., Erez, E., Nimrod, G. & Ben-Tal, N. (2009). Nucleic Acids Res. 37, D323-D327.
8. Heck, S. D. et al. (1994). Science, 266, 1065-1068.
9. Hett, E. C., Chao, M. C., Deng, L. L. & Rubin, E. J. (2008). PLoS Pathog. 4, e1000001.
10. Hett, E. C. & Rubin, E. J. (2008). Microbiol. Mol. Biol. Rev. 72, 126-156.
11. Kamphuis, I. G., Kalk, K. H., Swarte, M. B. & Drenth, J. (1984). J. Mol. Biol. 179, 233-256.
12. Kreil, G. (1994). Science, 266, 996-997.
13. Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R. & Thornton, J. M. (1996). J. Biomol. NMR, 8, 477-486.
14. Layec, S., Decaris, B. & Leblond-Bourget, N. (2008). Res. Microbiol. 159, 507-515.
15. Layec, S., Gérard, J., Legué, V., Chapot-Chartier, M.-P., Courtin, P., Borges, F., Decaris, B. & Leblond-Bourget, N. (2009). Mol. Microbiol. 71, 1205-1217.
16. Lindorff-Larsen, K., Piana, S., Palmo, K., Maragakis, P., Klepeis, J. L., Dror, R. O. & Shaw, D. E. (2010). Proteins, 78, 1950-1958.
17. Martínez-Caballero, S., Lee, M., Artola-Recolons, C., Carrasco-López, C., Hesek, D., Spink, E., Lastochkin, E., Zhang, W., Hellman, L. M., Boggess, B., Mobashery, S. & Hermoso, J. A. (2013). J. Am. Chem. Soc. 135, 10318-10321.
18. Meroueh, S. O., Bencze, K. Z., Hesek, D., Lee, M., Fisher, J. F., Stemmler, T. L. & Mobashery, S. (2006). Proc. Natl Acad. Sci. USA, 103, 4404-4409.
19. Murshudov, G. N., Skubák, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M. D., Long, F. & Vagin, A. A. (2011). Acta Cryst. D67, 355-367.
20. Nikitushkin, V. D., Demina, G. R., Shleeva, M. O. & Kaprelyants, A. S. (2013). Antonie Van Leeuwenhoek, 103, 37-46.
21. Otwinowski, Z. & Minor,W. (1997). Methods Enzymol. 276, 307-326.
22. Rossi, P., Aramini, J. M., Xiao, R., Chen, C. X., Nwosu, C., Owens, L. A., Maglaqui, M., Nair, R., Fischer, M., Acton, T. B., Honig, B., Rost, B. & Montelione, G. T. (2009). Proteins, 74, 515-519.
23. Ruggiero, A., De Simone, P., Smaldone, G., Squeglia, F. & Berisio, R. (2012). Curr. Protein Pept. Sci. 13, 756-766.
24. Ruggiero, A., Marasco, D., Squeglia, F., Soldini, S., Pedone, E., Pedone, C. & Berisio, R. (2010). Structure, 18, 1184-1190.
25. Ruggiero, A., Marchant, J., Squeglia, F., Makarov, V., De Simone, A. & Berisio, R. (2013). J. Biomol. Struct. Dyn. 31, 195-205.
26. Ruggiero, A., Squeglia, F., Esposito, C., Marasco, D., Pedone, E., Pedone, C. & Berisio, R. (2010). Protein Pept. Lett. 17, 70-73.
27. Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.
28. Squeglia, F., Marchetti, R., Ruggiero, A., Lanzetta, R., Marasco, D., Dworkin, J., Petoukhov, M., Molinaro, A., Berisio, R. & Silipo, A. (2011). J. Am. Chem. Soc. 133, 20676-20679.
29. Squeglia, F., Romano,M., Ruggiero, A., Vitagliano, L., De Simone, A. & Berisio, R. (2013). Biophys. J. 104, 2530-2539.
30. Storer, A. C. & Ménard, R. (1994). Methods Enzymol. 244, 486-500.
31. Tomiyama, T., Asano, S., Furiya, Y., Shirasawa, T., Endo, N. & Mori, H. (1994). J. Biol. Chem. 269, 10205-10208.
32. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.
33. Xu, Q. et al. (2010). Acta Cryst. F66, 1354-1364.
34. Biochemistry