Tyrosine latching of a regulatory gate affords allosteric control of aromatic amino acid biosynthesis

Journal of Biological Chemistry

Volumn 286, Issue 12, 2011, Pages 10216-10224

  Cross, Penelope J ^a   Dobson, Renwick C J ^a,b   Patchett, Mark L ^c   Parker, Emily J ^a  

^a UNIVERSITY OF CANTERBURY   (New Zealand)

^b UNIVERSITY OF MELBOURNE   (Australia)

^c MASSEY UNIVERSITY   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC CONTROL; ALLOSTERIC INHIBITION; AROMATIC AMINO ACID; CONTROLLED GATING; MONOMER UNITS; N-TERMINAL DOMAINS; REGULATORY DOMAIN; SHIKIMATE PATHWAY; SMALL ANGLE X-RAY SCATTERING; SYNTHASES; TETRAMERS; THERMOTOGA MARITIMA; WILD TYPES; WILD-TYPE ENZYMES;

AROMATIC COMPOUNDS; BIOCHEMISTRY; BIOSYNTHESIS; CONFORMATIONS; ENZYMES; MONOMERS; OLIGOMERS;

AMINO ACIDS;

3 DEOXY 7 PHOSPHOHEPTULONATE SYNTHASE; PHENYLALANINE; TRYPTOPHAN; TYROSINE;

ALLOSTERISM; AMINO ACID SYNTHESIS; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME MECHANISM; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE; THERMOTOGA MARITIMA; X RAY CRYSTALLOGRAPHY;

3-DEOXY-7-PHOSPHOHEPTULONATE SYNTHASE; ALLOSTERIC REGULATION; CRYSTALLOGRAPHY, X-RAY; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; THERMOTOGA MARITIMA; TYROSINE;

THERMOTOGA MARITIMA;

EID: 79953225494     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.209924     Document Type: Article

References (49)

1. Bentley, R. (1990) Crit. Rev. Biochem. Mol. Biol. 25, 307-384
2. Herrmann, K. M., and Weaver, L. M. (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol 50, 473-503
3. Herrmann, K. M., Zhao, J. M., Pinto, J. E. B. P., Weaver, L., and Henstrand, J. M. (1991) Curr. Top. Plant Physiol. 7, 12-18
4. Ogino, T., Garner, C., Markley, J. L., and Herrmann, K. M. (1982) Proc. Natl. Acad. Sci. U.S.A. 79, 5828-5832
5. Tribe, D. E., Camakaris, H., and Pittard, J. (1976) J. Bacteriol. 127, 1085-1097
6. Hoffmann, P. J., Doy, C. H., and Catcheside, D. E. A. (1972) Biochim. Biophys. Acta 268, 550-561
7. Hartmann, M., Schneider, T. R., Pfeil, A., Heinrich, G., Lipscomb, W. N., and Braus, G. H. (2003) Proc. Natl. Acad. Sci. U.S.A. 100, 862-867
8. Wu, J., and Woodard, R. W. (2006) J. Biol. Chem. 281, 4042-4048
9. Webby, C. J., Jiao, W., Hutton, R. D., Blackmore, N. J., Baker, H. M., Baker, E. N., Jameson, G. B., and Parker, E. J. (2010) J. Biol. Chem. 285, 30567-30576
10. Sasso, S., Okvist, M., Roderer, K., Gamper, M., Codoni, G., Krengel, U., and Kast, P. (2009) EMBO J. 28, 2128-2142
11. Walker, G. E., Dunbar, B., Hunter, I. S., Nimmo, H. G., and Coggins, J. R. (1996) Microbiology 142, 1973-1982
12. Jensen, R. A., Xie, G., Calhoun, D. H., and Bonner, C. A. (2002) J. Mol. Evol. 54, 416-423
13. Gosset, G., Bonner, C. A., and Jensen, R. A. (2001) J. Bacteriol. 183, 4061-4070
14. Shumilin, I. A., Zhao, C., Bauerle, R., and Kretsinger, R. H. (2002) J. Mol. Biol. 320, 1147-1156
15. Helmstaedt, K., Strittmatter, A., Lipscomb, W. N., and Braus, G. H. (2005) Proc. Natl. Acad. Sci. U.S.A. 102, 9784-9789
16. Schofield, L. R., Anderson, B. F., Patchett, M. L., Norris, G. E., Jameson, G. B., and Parker, E. J. (2005) Biochemistry 44, 11950-11962
17. Schofield, L. R., Patchett, M. L., and Parker, E. J. (2004) Protein Expr. Purif. 34, 17-27
18. Webby, C. J., Baker, H. M., Lott, J. S., Baker, E. N., and Parker, E. J. (2005) J. Mol. Biol. 354, 927-939
19. Wu, J., Howe, D. L., and Woodard, R. W. (2003) J. Biol. Chem. 278, 27525-27531
20. Shumilin, I. A., Bauerle, R., Wu, J., Woodard, R. W., and Kretsinger, R. H. (2004) J. Mol. Biol. 341, 455-466
21. Tabor, S., and Richardson, C. C. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 1074-1078
22. Schoner, R., and Herrmann, K. M. (1976) J. Biol. Chem. 251, 5440-5447
23. Leatherbarrow, R. J. (2007) Grafit, Version 6, Erithacus Software Ltd., Horly, United Kingdom
24. Steller, I., Bolotovsky, R., and Rossmann, M. G. (1997) J. Appl. Crystallogr. 30, 1036-1040
25. Evans, P. (2006) Acta Crystallogr. D Biol. Crystallogr. 62, 72-82
26. Storoni, L. C., McCoy, A. J., and Read, R. J. (2004) Acta Crystallogr. D Biol. Crystallogr. 60, 432-438
27. Bailey, S. (1994) Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
28. Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L. W., Kapral, G. J., Grosse-Kunstleve, R. W., Mc- Coy, A. J., Moriarty, N. W., Oeffner, R., Read, R. J., Richardson, D. C., Richardson, J. S., Terwilliger, T. C., and Zwart, P. H. (2010) Acta Crystallogr. D Biol. Crystallogr. 66, 213-221
29. Emsley, P., and Cowtan, K. (2004) Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132
30. Painter, J., and Merritt, E. A. (2006) J. Appl. Crystallogr. 39, 109-111
31. Chen, V. B., Arendall, W. B., 3rd, Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., and Richardson, D. C. (2010) Acta Crystallogr. D Biol. Crystallogr. 66, 12-21
32. DeLano, W. L. (2002) DeLano, W. L. (2002) The PyMOL Molecular Graphics System, DeLano Scientific LLC, San Carlos, CA
33. Deleted in proof
34. Svergun, D. I. (1992) J. Appl. Crystallogr. 25, 495-503
35. Svergun, D., Barberato, C., and Koch, M. H. (1995) J. Appl. Crystallogr. 28, 768-773
36. Mertens, H. D., and Svergun, D. I. (2010) J. Struct. Biol. 172, 128-141
37. Mills, R. D., Trewhella, J., Qiu, T. W., Welte, T., Ryan, T. M., Hanley, T., Knott, R. B., Lithgow, T., and Mulhern, T. D. (2009) J. Mol. Biol. 388, 1043-1058
38. Grant, G. A. (2006) J. Biol. Chem. 281, 33825-33829
39. Curien, G., Biou, V., Mas-Droux, C., Robert-Genthon, M., Ferrer, J. L., and Dumas, R. (2008) Plant Physiol. Biochem. 46, 325-339
40. Laskowski, R. A., Gerick, F., and Thornton, J. M. (2009) FEBS Lett. 583, 1692-1698
41. Liberles, J. S., Thórólfsson, M., and Martínez, A. (2005) Amino Acids 28, 1-12
42. Tang, C., Schwieters, C. D., and Clore, G. M. (2007) Nature 449, 1078-1082
43. Boehr, D. D., Nussinov, R., and Wright, P. E. (2009) Nat. Chem. Biol. 5, 789-796
44. Bakan, A., and Bahar, I. (2009) Proc. Natl. Acad. Sci. U.S.A. 106, 14349-14354
45. Hammes, G. G., Chang, Y. C., and Oas, T. G. (2009) Proc. Natl. Acad. Sci. U.S.A. 106, 13737-13741
46. Ma, B., and Nussinov, R. (2010) Curr. Opin. Chem. Biol. 14, 652-659
47. Cho, Y., Sharma, V., and Sacchettini, J. C. (2003) J. Biol. Chem. 278, 8333-8339
48. Zhang, S., Pohnert, G., Kongsaeree, P., Wilson, D. B., Clardy, J., and Ganem, B. (1998) J. Biol. Chem. 273, 6248-6253
49. Roberts, F., Roberts, C. W., Johnson, J. J., Kyle, D. E., Krell, T., Coggins, J. R., Coombs, G. H., Milhous, W. K., Tzipori, S., Ferguson, D. J., Chakrabarti, D., and McLeod, R. (1998) Nature 393, 801-805