Structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC118

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 68, Issue 12, 2012, Pages 1427-1433

  Lobley, Carina M C ^a   Aller, Pierre ^a   Douangamath, Alice ^a   Reddivari, Yamini ^b   Bumann, Mario ^c   Bird, Louise E ^b   Nettleship, Joanne E ^b   Brandao Neto, Jose ^a   Owens, Raymond J ^b   Otoole, Paul W ^d   Walsh, Martin A ^a,c  

^a DIAMOND LIGHT SOURCE LTD   (United Kingdom)

^b RUTHERFORD APPLETON LABORATORY   (United Kingdom)

^c EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

^d UNIVERSITY COLLEGE CORK   (Ireland)

Author keywords

in situ diffraction; Lactobacillus salivarius; ribose 5 phosphate isomerase

Indexed keywords

ISOMERASE; RIBOSEPHOSPHATE ISOMERASE;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CHEMISTRY; DIMERIZATION; ENZYMOLOGY; LACTOBACILLUS; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

ALDOSE-KETOSE ISOMERASES; AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; LACTOBACILLUS; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE ALIGNMENT;

BACTERIA (MICROORGANISMS); LACTOBACILLUS SALIVARIUS;

EID: 84870932740     PISSN: None     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S174430911204273X     Document Type: Article

References (51)

1. Axford, D. et al. (2012). Acta Cryst. D68, 592-600.
2. Berman, H., Henrick, K. & Nakamura, H. (2003). Nature Struct. Biol. 10, 980.
3. Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N. & Bourne, P. E. (2000). Nucleic Acids Res. 28, 235-242.
4. Berrow, N. S., Alderton, D., Sainsbury, S., Nettleship, J., Assenberg, R., Rahman, N., Stuart, D. I. & Owens, R. J. (2007). Nucleic Acids Res. 35, e45.
5. Bingel-Erlenmeyer, R., Olieric, V., Grimshaw, J. P. A., Gabadinho, J.,Wang, X., Ebner, S. G., Isenegger, A., Schneider, R., Schneider, J., Glettig, W., Pradervand, C., Panepucci, E. H., Tomizaki, T., Wang, M. & Schulze-Briese, C. (2011). Cryst. Growth Des. 11, 916-923.
6. Bird, L. E. (2011). Methods, 55, 29-37.
7. 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.
8. Corr, S. C., Li, Y., Riedel, C. U., O'Toole, P. W., Hill, C. & Gahan, C. G. (2007). Proc. Natl Acad. Sci. USA, 104, 7617-7621.
9. Edwards, T. E., Abramov, A. B., Smith, E. R., Baydo, R. O., Leonard, J. T., Leibly, D. J., Thompkins, K. B., Clifton, M. C., Gardberg, A. S., Staker, B. L., Van Voorhis, W. C., Myler, P. J. & Stewart, L. J. (2011). BMC Struct. Biol. 11, 39.
10. Emsley, P. & Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
11. Evans, P. (2006). Acta Cryst. D62, 72-82.
12. Evrard, G. X., Langer, G. G., Perrakis, A. & Lamzin, V. S. (2007). Acta Cryst. D63, 108-117.
13. Gorrec, F. (2009). J. Appl. Cryst. 42, 1035-1042.
14. Graille, M., Meyer, P., Leulliot, N., Sorel, I., Janin, J., Van Tilbeurgh, H. & Quevillon-Cheruel, S. (2005). Biochimie, 87, 763-769.
15. Hamada, K., Ago, H., Sugahara, M., Nodake, Y., Kuramitsu, S. & Miyano, M. (2003). J. Biol. Chem. 278, 49183-49190.
16. Hargreaves, D. (2012). J. Appl. Cryst. 45, 138-140.
17. Holmes, M. A. et al. (2006). Acta Cryst. F62, 427-431.
18. Ishikawa, K., Matsui, I., Payan, F., Cambillau, C., Ishida, H., Kawarabayasi, Y., Kikuchi, H. & Roussel, A. (2002). Structure, 10, 877-886.
19. Jacquamet, L., Joly, J., Bertoni, A., Charrault, P., Pirocchi, M., Vernede, X., Bouis, F., Borel, F., Pé rin, J.-P., Denis, T., Rechatin, J.-L. & Ferrer, J.-L. (2009). J. Synchrotron Rad. 16, 14-21.
20. Jacquamet, L., Ohana, J., Joly, J., Borel, F., Pirocchi, M., Charrault, P., Bertoni, A., Israel-Gouy, P., Carpentier, P., Kozielski, F., Blot, D. & Ferrer, J.-L. (2004). Structure, 12, 1219-1225.
21. Jung, J., Kim, J.-K., Yeom, S.-J., Ahn, Y.-J., Oh, D.-K. & Kang, L.-W. (2011). Appl. Microbiol. Biotechnol. 90, 517-527.
22. Keegan, R. M. & Winn, M. D. (2007). Acta Cryst. D63, 447-457.
23. Kim, T. G., Kwon, T. H., Min, K., Dong, M.-S., Park, Y. I. & Ban, C. (2009). Mol. Cells, 27, 99-103.
24. Krissinel, E. & Henrick, K. (2007). J. Mol. Biol. 372, 774-797.
25. Leslie, A. G. W. (2006). Acta Cryst. D62, 48-57.
26. Maire, A. le, Gelin, M., Pochet, S., Hoh, F., Pirocchi, M., Guichou, J.-F., Ferrer, J.-L. & Labesse, G. (2011). Acta Cryst. D67, 747-755.
27. Murshudov, G. N., Skubá k, 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.
28. Murzin, A. G., Brenner, S. E., Hubbard, T. & Chothia, C. (1995). J. Mol. Biol. 247, 536-540.
29. Neville, B. A. & O'Toole, P. W. (2010). Future Microbiol. 5, 759-774.
30. Nicholls, R. A. (2011). PhD thesis. University of York.
31. Nichols, C. E., Sainsbury, S., Ren, J., Walter, T. S., Verma, A., Stammers, D. K., Saunders, N. J. & Owens, R. J. (2009). Acta Cryst. F65, 204-209.
32. O'Callaghan, J., Buttó, L. F., MacSharry, J., Nally, K. & O'Toole, P. W. (2012). Appl. Environ. Microbiol. 78, 5196-5203.
33. Ohana, J., Jacquamet, L., Joly, J., Bertoni, A., Taunier, P., Michel, L., Charrault, P., Pirocchi, M., Carpentier, P., Borel, F., Kahn, R. & Ferrer, J.-L. (2004). J. Appl. Cryst. 37, 72-77.
34. Pearson, W. R. & Lipman, D. J. (1988). Proc. Natl Acad. Sci. USA, 85, 2444- 2448.
35. Pei, J., Kim, B.-H. & Grishin, N. V. (2008). Nucleic Acids Res. 36, 2295-2300.
36. Rangarajan, E. S., Sivaraman, J., Matte, A. & Cygler, M. (2002). Proteins, 48, 737-740.
37. Roos, A. K., Andersson, C. E., Bergfors, T., Jacobsson, M., Karlé n, A., Unge, T., Jones, T. A. & Mowbray, S. L. (2004). J. Mol. Biol. 335, 799-809.
38. Roos, A. K., Burgos, E., Ericsson, D. J., Salmon, L. & Mowbray, S. L. (2005). J. Biol. Chem. 280, 6416-6422.
39. Sauter, N. K., Grosse-Kunstleve, R. W. & Adams, P. D. (2004). J. Appl. Cryst. 37, 399-409.
40. Stein, N. (2008). J. Appl. Cryst. 41, 641-643.
41. Stern, A. L., Naworyta, A., Cazzulo, J. J. & Mowbray, S. L. (2011). FEBS J. 278, 793-808.
42. Strange, R. W., Antonyuk, S. V., Ellis, M. J., Bessho, Y., Kuramitsu, S., Yokoyama, S. & Hasnain, S. S. (2009). Acta Cryst. F65, 1214-1217.
43. Studier, F. W. (2005). Protein Expr. Purif. 41, 207-234.
44. Vagin, A. & Teplyakov, A. (2010). Acta Cryst. D66, 22-25.
45. Walter, T. S. et al. (2005). Acta Cryst. D61, 651-657.
46. Wang, X. et al. (2012). Nature Struct. Mol. Biol. 19, 424-429.
47. Winter, G. (2010). J. Appl. Cryst. 43, 186-190.
48. Xu, Q. et al. (2004). Proteins, 56, 171-175.
49. Zhang, R., Andersson, C. E., Savchenko, A., Skarina, T., Evdokimova, E., Beasley, S., Arrowsmith, C. H., Edwards, A.M., Joachimiak, A. &Mowbray, S. L. (2003). Structure, 11, 31-42.
50. Zhang, R. G., Andersson, C. E., Skarina, T., Evdokimova, E., Edwards, A. M., Joachimiak, A., Savchenko, A. & Mowbray, S. L. (2003). J. Mol. Biol. 332, 1083-1094.
51. Zhang, Z., Sauter, N. K., van den Bedem, H., Snell, G. & Deacon, A. M. (2006). J. Appl. Cryst. 39, 112-119.