Structure of the N-terminal domain of the effector protein LegC3 from Legionella pneumophila

Acta Crystallographica Section D: Biological Crystallography

Volumn 70, Issue 2, 2014, Pages 436-441

  Yao, Deqiang ^a,c   Cherney, Maia ^a   Cygler, Miroslaw ^a,b  

^a UNIVERSITY OF SASKATCHEWAN   (Canada)

^b MCGILL UNIVERSITY   (Canada)

^c INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

Author keywords

effector proteins; LegC3; Legionella pneumophila

Indexed keywords

BACTERIAL PROTEIN; RECOMBINANT PROTEIN;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; EFFECTOR PROTEINS; ESCHERICHIA COLI; GENETICS; LEGC3; LEGIONELLA PNEUMOPHILA; METABOLISM; MOLECULAR GENETICS; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

EFFECTOR PROTEINS; LEGC3; LEGIONELLA PNEUMOPHILA;

AMINO ACID MOTIFS; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; LEGIONELLA PNEUMOPHILA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS;

EID: 84894146880     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S139900471302991X     Document Type: Article

References (19)

1. Adams, P. D. et al. (2010). Acta Cryst. D66, 213-221.
2. Bennett, T. L., Kraft, S. M., Reaves, B. J., Mima, J., O'Brien, K. M. & Starai, V. J. (2013). PLoS One, 8, e56798.
3. Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S. & Richardson, D. C. (2010). Acta Cryst. D66, 12-21.
4. Emsley, P. & Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
5. De Felipe, K. S., Glover, R. T., Charpentier, X., Anderson, O. R., Reyes, M., Pericone, C. D. & Shuman, H. A. (2008). PLoS Pathog. 4, e1000117.
6. Gomez-Valero, L., Rusniok, C., Jarraud, S., Vacherie, B., Rouy, Z., Barbe, V., Medigue, C., Etienne, J. & Buchrieser, C. (2011). BMC Genomics, 12, 536.
7. Grochulski, P., Fodje, M. N., Gorin, J., Labiuk, S. L. & Berg, R. (2011). J. Synchrotron Rad. 18, 681-684.
8. He, Y., Yao, D.-Q., Gu, Y.-X., Lin, Z.-J., Zheng, C.-D. & Fan, H.-F. (2007). Acta Cryst. D63, 793-799.
9. Hendrickson, W. A., Horton, J. R. & Le Master, D. M. (1990). EMBO J. 9, 1665-1672.
10. Holm, L. & Sander, C. (1995). Trends Biochem. Sci. 20, 478-480.
11. Hubber, A. & Roy, C. R. (2010). Annu. Rev. Cell Dev. Biol. 26, 261-283.
12. Isberg, R. R., O'Connor, T. J. & Heidtman, M. (2009). Nature Rev. Microbiol. 7, 13-24.
13. Kliche, W., Fujita-Becker, S., Kollmar, M., Manstein, D. J. & Kull, F. J. (2001). EMBO J. 20, 40-46.
14. Marín, M., Uversky, V. N. & Ott, T. (2013). Plant Cell, 25, 3153-3157.
15. Mueller, M., Grauschopf, U., Maier, T., Glockshuber, R. & Ban, N. (2009). Nature (London), 459, 726-730.
16. Pieper, U., Eswar, N., Davis, F. P., Braberg, H., Madhusudhan, M. S., Rossi, A., Marti-Renom, M., Karchin, R., Webb, B. M., Eramian, D., Shen, M. Y., Kelly, L., Melo, F. & Sali, A. (2006). Nucleic Acids Res. 34, D291-D295.
17. Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.
18. Vogel, J. P. & Isberg, R. R. (1999). Curr. Opin. Microbiol. 2, 30-34.
19. Xie, W., Yang, X., Xu, M. & Jiang, T. (2012). Protein Cell, 3, 864-874.