The structure of Serratia marcescens Lip, a membrane-bound component of the type VI secretion system

Acta Crystallographica Section D: Biological Crystallography

Volumn 67, Issue 12, 2011, Pages 1065-1072

  Rao, Vincenzo A ^a   Shepherd, Sharon M ^a   English, Grant ^a   Coulthurst, Sarah J ^a   Hunter, William N ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

Author keywords

sandwich; Gram negative pathogens; lipoproteins; protein secretion; transthyretin; virulence

Indexed keywords

BACTERIAL PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; SERRATIA MARCESCENS; STRUCTURAL HOMOLOGY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SERRATIA MARCESCENS; STRUCTURAL HOMOLOGY, PROTEIN;

EID: 82455210505     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444911046300     Document Type: Article

References (48)

1. Adams, P. D. et al. (2010). Acta Cryst. D66, 213-221.
2. Aschtgen, M. S., Bernard, C. S., De Bentzmann, S., Lloubès, R. & Cascales, E. (2008). J. Bacteriol. 190, 7523-7531.
3. Blake, C. C., Geisow, M. J., Oatley, S. J., Rérat, B. & Rérat, C. (1978). J. Mol. Biol. 121, 339-356.
4. Blondel, C. J., Yang, H.-J., Castro, B., Chiang, S., Toro, C. S., Zald?́var, M., Contreras, I., Andrews-Polymenis, H. L. & Santiviago, C. A. (2010). PLoS One, 5, e11724.
5. Bond, C. S. & Schüttelkopf, A. W. (2009). Acta Cryst. D65, 510-512.
6. Bönemann, G., Pietrosiuk, A. & Mogk, A. (2010). Mol. Microbiol. 76, 815-821.
7. Bos, M. P., Robert, V. & Tommassen, J. (2007). Annu. Rev. Microbiol. 61, 191-214.
8. Cascales, E. (2008). EMBO Rep. 9, 735-741.
9. 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.
10. Cruickshank, D. W. J. (1999). Acta Cryst. D55, 583-601.
11. Di Tommaso, P., Moretti, S., Xenarios, I., Orobitg, M., Montanyola, A., Chang, J.-M., Taly, J.-F. & Notredame, C. (2011). Nucleic Acids Res. 39, W13-W17.
12. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. (2010). Acta Cryst. D66, 486-501.
13. Eneqvist, T., Lundberg, E., Karlsson, A., Huang, S., Santos, C. R., Power, D. M. & Sauer-Eriksson, A. E. (2004). J. Biol. Chem. 279, 26411-26416.
14. Engh, R. A. & Huber, R. (1991). Acta Cryst. A47, 392-400.
15. Evans, P. (2006). Acta Cryst. D62, 72-82.
16. Filloux, A., Hachani, A. & Bleves, S. (2008). Microbiology, 154, 1570-1583.
17. French, J. B. & Ealick, S. E. (2011). Acta Cryst. D67, 671-677.
18. Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M. R., Appel, R. D. & Bairoch, A. (2005). The Proteomics Protocols Handbook, edited by J. M. Walker, pp. 571-607. Totowa: Humana Press.
19. Gerlach, R. G. & Hensel, M. (2007). Int. J. Med. Microbiol. 297, 401-415.
20. Hatzixanthis, K., Palmer, T. & Sargent, F. (2003). Mol. Microbiol. 49, 1377-1390.
21. Hejazi, A. & Falkiner, F. R. (1997). J. Med. Microbiol. 46, 903-912.
22. Hennebry, S. C. (2009). FEBS J. 276, 5367-5379.
23. Hennebry, S. C., Law, R. H., Richardson, S. J., Buckle, A. M. & Whisstock, J. C. (2006). J. Mol. Biol. 359, 1389-1399.
24. Holland, I. B. (2010). Methods Mol. Biol. 619, 1-20.
25. Hood, R. D. et al. (2010). Cell Host Microbe, 7, 25-37.
26. Jani, A. J. & Cotter, P. A. (2010). Cell Host Microbe, 8, 2-6.
27. Juncker, A. S., Willenbrock, H., Von Heijne, G., Brunak, S., Nielsen, H. & Krogh, A. (2003). Protein Sci. 12, 1652-1662.
28. Kabsch, W. (2010). Acta Cryst. D66, 125-132.
29. Kabsch, W. & Sander, C. (1983). Biopolymers, 22, 2577-2637.
30. Karimova, G., Pidoux, J., Ullmann, A. & Ladant, D. (1998). Proc. Natl Acad. Sci. USA, 95, 5752-5756.
31. Karimova, G., Ullmann, A. & Ladant, D. (2000). Methods Enzymol. 328, 59-73.
32. Karimova, G., Ullmann, A. & Ladant, D. (2001). J. Mol. Microbiol. Biotechnol. 3, 73-82.
33. Krissinel, E. & Henrick, K. (2007). J. Mol. Biol. 372, 774-797.
34. Laskowski, R. A., Watson, J. D. & Thornton, J. M. (2005). Nucleic Acids Res. 33, W89-W93.
35. Liu, H., Coulthurst, S. J., Pritchard, L., Hedley, P. E., Ravensdale, M., Humphris, S., Burr, T., Takle, G., Brurberg, M. B., Birch, P. R., Salmond, G. P. & Toth, I. K. (2008). PLoS Pathog. 4, e1000093.
36. MacIntyre, D. L., Miyata, S. T., Kitaoka, M. & Pukatzki, S. (2010). Proc. Natl Acad. Sci. USA, 107, 19520-19524.
37. McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C. & Read, R. J. (2007). J. Appl. Cryst. 40, 658-674.
38. Monaco, H. L., Rizzi, M. & Coda, A. (1995). Science, 268, 1039-1041.
39. Murdoch, S. L., Trunk, K., English, G., Fritsch, M. J., Pourkarimi, E. & Coulthurst, S. J. (2011). J. Bacteriol. 193, 6057-6069.
40. 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.
41. Pukatzki, S., McAuley, S. B. & Miyata, S. T. (2009). Curr. Opin. Microbiol. 12, 11-17.
42. Sarris, P. F., Skandalis, N., Kokkinidis, M. & Panopoulos, N. J. (2010). Mol. Plant Pathol. 11, 795-804.
43. Schwarz, S., Hood, R. D. & Mougous, J. D. (2010). Trends Microbiol. 18, 531-537.
44. Studier, F. W. (2005). Protein Expr. Purif. 41, 207-234.
45. Terwilliger, T. C. (2003). Acta Cryst. D59, 38-44.
46. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.
47. Wojtczak, A., Luft, J. & Cody, V. (1992). J. Biol. Chem. 267, 353-357.
48. Zanotti, G., Folli, C., Cendron, L., Alfieri, B., Nishida, S. K., Gliubich, F., Pasquato, N., Negro, A. & Berni, R. (2008). FEBS J. 275, 5841-5854.