The structure of Haemophilus influenzae prephenate dehydrogenase suggests unique features of bifunctional TyrA enzymes

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 66, Issue 10, 2010, Pages 1317-1325

  Chiu, Hsiu Ju ^a,b   Abdubek, Polat ^b,c   Astakhova, Tamara ^b,d   Axelrod, Herbert L ^a,b   Carlton, Dennis ^b,e   Clayton, Thomas ^b,e   Das, Debanu ^a,b   Deller, Marc C ^b,e   Duan, Lian ^b,d   Feuerhelm, Julie ^b,c   Grant, Joanna C ^b,c   Grzechnik, Anna ^b,e   Han, Gye Won ^b,e   Jaroszewski, Lukasz ^b,d,f   Jin, Kevin K ^a,b   Klock, Heath E ^b,c   Knuth, Mark W ^b,c   Kozbial, Piotr ^b,f   Krishna, S Sri ^b,d,f   Kumar, Abhinav ^a,b   Marciano, David ^b,e   McMullan, Daniel ^b,c   Miller, Mitchell D ^a,b   Morse, Andrew T ^b,d   Nigoghossian, Edward ^b,c   Okach, Linda ^b,c   Reyes, Ron ^a,b   Tien, Henry J ^b,e   Trame, Christine B ^a,b   Van Den Bedem, Henry ^a,b   Weekes, Dana ^b,f   Xu, Qingping ^a,b   Hodgson, Keith O ^b,g   Wooley, John ^b,d   Elsliger, Marc André ^b,e   Deacon, Ashley M ^a,b   Godzik, Adam ^b,d,f   Lesley, Scott A ^b,c,e   Wilson, Ian A ^b,e   more..

^a SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

^b Joint Center for Structural Genomics   (United States)

^c GENOMICS INSTITUTE OF THE NOVARTIS RESEARCH FOUNDATION   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

^e SCRIPPS RESEARCH INSTITUTE   (United States)

^f BURNHAM INSTITUTE   (United States)

^g SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

Author keywords

chorismate; Haemophilus influenzae; prephenate; structural genomics; tyrosine biosynthesis

Indexed keywords

BACTERIAL PROTEIN; MULTIENZYME COMPLEX; PREPHENATE DEHYDROGENASE; TYRA PROTEIN, BACTERIA;

ARTICLE; CHEMISTRY; ENZYMOLOGY; HAEMOPHILUS INFLUENZAE; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; HAEMOPHILUS INFLUENZAE; MULTIENZYME COMPLEXES; PREPHENATE DEHYDROGENASE;

HAEMOPHILUS INFLUENZAE; HAEMOPHILUS INFLUENZAE RD KW20; SYNECHOCYSTIS; SYNECHOCYSTIS SP.;

EID: 77958041941     PISSN: 17443091     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309110021688     Document Type: Article

References (53)

1. Ahmad, S. & Jensen, R. A. (1987). FEBS Lett. 216, 133-139.
2. Beller, H. R., Chain, P. S., Letain, T. E., Chakicherla, A., Larimer, F. W., Richardson, P. M., Coleman, M. A., Wood, A. P. & Kelly, D. P. (2006). J. Bacteriol. 188, 1473-1488.
3. Bonvin, J., Aponte, R. A., Marcantonio, M., Singh, S., Christendat, D. & Turnbull, J. L. (2006). Protein Sci. 15, 1417-1432.
4. Calhoun, D. H., Bonner, C. A., Gu, W., Xie, G. & Jensen, R. A. (2001). Genome Biol. 2, 1-16.
5. Champney, W. S. & Jensen, R. A. (1970). J. Biol. Chem. 245, 3763-3770.
6. 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.
7. Chipman, D. M. & Shaanan, B. (2001). Curr. Opin. Struct. Biol. 11, 694-700.
8. Christendat, D., Saridakis, V. C. & Turnbull, J. L. (1998). Biochemistry, 37, 15703-15712.
9. Christendat, D. & Turnbull, J. L. (1999). Biochemistry, 38, 4782-4793.
10. Christopherson, R. I. (1985). Arch. Biochem. Biophys. 240, 646-654.
11. Cobbett, C. S. & Delbridge, M. L. (1987). J. Bacteriol. 169, 2500-2506.
12. Cohen, A. E., Ellis, P. J., Miller, M. D., Deacon, A. M. & Phizackerley, R. P. (2002). J. Appl. Cryst. 35, 720-726.
13. Cohen, S. X., Morris, R. J., Fernandez, F. J., Ben Jelloul, M., Kakaris, M., Parthasarathy, V., Lamzin, V. S., Kleywegt, G. J. & Perrakis, A. (2004). Acta Cryst. D60, 2222-2229.
14. Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.
15. Cruickshank, D. W. J. (1999). Acta Cryst. D55, 583-601.
16. Diederichs, K. & Karplus, P. A. (1997). Nature Struct. Biol. 4, 269-275.
17. DeLano, W. L. (2002). PyMOL Molecular Viewer. DeLano Scientific LLC, Palo Alto, California, USA. http://www.pymol.org.
18. Emsley, P. & Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
19. Grant, G. A. (2006). J. Biol. Chem. 281, 33825-33829.
20. Hermes, J. D., Tipton, P. A., Fisher, M. A., O'Leary, M. H., Morrison, J. F. & Cleland, W. W. (1984). Biochemistry 23, 6263-6275.
21. Kabsch, W. (1993). J. Appl. Cryst. 26, 795-800.
22. Kabsch, W. (2010a). Acta Cryst. D66, 125-132.
23. Kabsch, W. (2010b). Acta Cryst. D66, 133-144.
24. Kleywegt, G. J. (2000). Acta Cryst. D56, 249-265.
25. Klock, H. E., Koesema, E. J., Knuth, M.W. & Lesley, S. A. (2008). Proteins, 71, 982-994.
26. Krishna, S. S.,Weekes, D., Bakolitsa, C., Elsliger, M.-A.,Wilson, I. A., Godzik, A. & Wooley, J. (2010). Acta Cryst. F66, 1143-1147.
27. Krissinel, E. & Henrick, K. (2005). CompLife 2005, edited by M. R. Berthold, R. Glen, K. Diederichs, O. Kohlbacher & I. Fischer, pp. 163-174. Berlin/ Heidelberg: Springer-Verlag.
28. Laskowski, R. A. (2009). Nucleic Acids Res. 37, D355-D359.
29. Legrand, P., Dumas, R., Seux, M., Rippert, P., Ravelli, R., Ferrer, J.-L. & Matringe, M. (2006). Structure, 14, 767-776.
30. Lesley, S. A. et al. (2002). Proc. Natl Acad. Sci. USA, 99, 11664-11669.
31. Matthews, B. W. (1968). J. Mol. Biol. 33, 491-497.
32. Rippert, P. & Matringe, M. (2002). Eur. J. Biochem. 269, 4753-4761.
33. Sampathkumar, P. & Morrison, J. F. (1982). Biochim. Biophys. Acta, 702, 212-219.
34. Santarsiero, B. D., Yegian, D. T., Lee, C. C., Spraggon, G., Gu, J., Scheibe, D., Uber, D. C., Cornell, E. W., Nordmeyer, R. A., Kolbe, W. F., Jin, J., Jones, A. L., Jaklevic, J.M., Schultz, P. G. & Stevens, R. C. (2002). J. Appl. Cryst. 35, 278-281.
35. Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.
36. Song, J., Bonner, C. A., Wolinsky, M. & Jensen, R. A. (2005). BMC Biol. 3, 13.
37. Sun, W., Shahinas, D., Bonvin, J., Hou, W., Kimber, M. S., Turnbull, J. & Christendat, D. (2009). J. Biol. Chem. 284, 13223-13232.
38. Sun, W., Singh, S., Zhang, R., Turnbull, J. L. & Christendat, D. (2006). J. Biol. Chem. 281, 12919-12928.
39. Terwilliger, T. (2004). J. Synchrotron Rad. 11, 49-52.
40. Thompson, J. D., Higgins, D. G. & Gibson, T. J. (1994). Nucleic Acids Res. 22, 4673-4680.
41. Turnbull, J., Cleland, W. W. & Morrison, J. F. (1990). Biochemistry, 29, 10245-10254.
42. Turnbull, J., Cleland, W. W. & Morrison, J. F. (1991). Biochemistry, 30, 7777-7782.
43. Turnbull, J., Morrison, J. F. & Cleland, W. W. (1991). Biochemistry 30, 7783-7788.
44. Vaguine, A. A., Richelle, J. & Wodak, S. J. (1999). Acta Cryst. D55, 191-205.
45. Van Duyne, G. D., Standaert, R. F., Karplus, P. A., Schreiber, S. L. & Clardy, J. (1993). J. Mol. Biol. 229, 105-124.
46. Vonrhein, C., Blanc, E., Roversi, P. & Bricogne, G. (2007). Methods Mol. Biol. 364, 215-230.
47. Vriend, G. (1990). J. Mol. Graph. 8, 52-56.
48. Winn, M. D., Murshudov, G. N. & Papiz, M. Z. (2003). Methods Enzymol. 374, 300-321.
49. Xia, T. & Jensen, R. A. (1990). J. Biol. Chem. 265, 20033-20036.
50. Xie, G., Bonner, C. A. & Jensen, R. A. (2000). Comput. Biochem. Physiol. C Toxicol. Pharmacol. 125, 65-83.
51. Yang, H., Guranovic, V., Dutta, S., Feng, Z., Berman, H. M. & Westbrook, J. D. (2004). Acta Cryst. D60, 1833-1839.
52. Ye, Y. & Godzik, A. (2004). Nucleic Acids Res. 32, W582-W585.
53. Zhao, G., Xia, T., Ingram, L. O. & Jensen, R. A. (1993). Eur. J. Biochem. 212, 157-165.