Structure of a transiently phosphorylated switch in bacterial signal transduction

Nature

Volumn 402, Issue 6764, 1999, Pages 894-897

  Kern, Dorothee ^a   Volkman, Brian F ^b   Luginbuhl, Peter ^c   Nohaile, Michael J ^c   Kustu, Sydney ^d   Wemmer, David E ^c  

^a BRANDEIS UNIVERSITY   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; REGULATOR PROTEIN;

ARTICLE; AUTOPHOSPHORYLATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DEPHOSPHORYLATION; ESCHERICHIA COLI; GENETIC TRANSCRIPTION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; SIGNAL NOISE RATIO; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS; TRANSCRIPTION INITIATION;

BACTERIAL PROTEINS; BINDING SITES; DNA-BINDING PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PHOSPHORYLATION; PII NITROGEN REGULATORY PROTEINS; PROTEIN CONFORMATION; SIGNAL TRANSDUCTION; TRANS-ACTIVATORS; TRANSCRIPTION FACTORS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA; PROKARYOTA;

EID: 0033599026     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/47273     Document Type: Article

References (29)

1. Parkinson, J. S. & Kofoid, E. C. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26, 71-112 (1992).
2. Stock, J. B., Surette, M. G., Levit, M. & Park, P. in Two-Component Signal Transduction (eds Hoch, J. A. & Silhavy, T. J.) 25-51 (American Society for Microbiology, Washington DC, 1995).
3. Stock, A. M., Mottonen, J. M., Stock, J. B. & Schutt, C. E. Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis. Nature 337, 745-749 (1989).
4. Baikalov, I. et al. Structure of the Escherichia coli response regulator NarL. Biochemistry 35, 11053-11061 (1996).
5. Volkman, B. F., Nohaile, M. J., Amy, N. K., Kustu, S. & Wemmer, D. E. Three-dimensional solution structure of the N-terminal receiver domain of NTRC. Biochemistry 34, 1413-1424 (1995).
6. Feher, V. A. et al. High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition. Biochemistry 36, 10015-10025 (1997).
7. Djordjevic, S., Goudreau, P. N., Xu, Q. P., Stock, A. M. & West, A. H. Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain. Proc. Natl Acad. Sci. USA 95, 1381-1386 (1998).
8. Sola, M., Gomis-Ruth, F. X., Serrano, L., Gonzalez, A. & Coll, M. Three-dimensional crystal structure of the transcription factor PhoB receiver domain. J. Mol. Biol. 285, 675-687 (1999).
9. Novak, R., Henriques, B., Charpentier, E., Normark, S. & Tuomanen, E. Emergence of vancomycin tolerance in Streptococcus pneumoniae. Nature 399, 590-593 (1999).
10. Rombel, I., North, A., Hwang, I., Wyman, C. & Kustu, S. in Cold Spring Harbor Symposia on Quantitative Biology: Mechanisms of Transcription (ed. Brown, D.) 157-166 (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, 1998).
11. Nohaile, M., Kern, D., Wemmer, D., Stedman, K. & Kustu, S. Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: evidence for an activating surface. J. Mol. Biol. 273, 299-316 (1997).
12. 19F MMR and protein engineering. J. Biol. Chem. 268, 13081-13088 (1993).
13. Lowry, D. F. et al. Signal transduction in chemotaxis. A propagating conformation change upon phosphorylation of CheY. J. Biol. Chem. 269, 26358-26362 (1994).
14. Lukat, G. S., McCleary, W. R., Stock, A. M. & Stock, J. B. Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors. Proc. Natl Acad. Sci. USA 89, 718-722 (1992).
15. Hwang, I., Thorgeirsson, T., Lee, J., Kustu, S. & Shin, Y.-K. Physical evidence for a phosphorylation-dependent conformational change in the enhancer-binding protein NtrC. Proc. Natl Acad. Sci. USA 96, 4880-4885 (1999).
16. Volz, K. Structural conservation in the CheY superfamily. Biochemistry 32, 11741-11753 (1993).
17. Slock, A. M. et al. Structure of the Mg(2+)-bound form of CheY and mechanisms of phosphoryl transfer in bacterial chemotaxis. Biochemistry 32, 13375-13380 (1993).
18. Bellsolell, L., Prieto, J., Serrano, L. & Coll, M. Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface. J. Mol. Biol. 238, 489-495 (1994).
19. Santoro, J., Bruix, M., Pascual, J., López, E., Serrano, L. & Rico, M. 3-Dimensional structure of chemotactic Che-Y protein in aqueous-solution by nuclear-magnetic-resonance methods. J. Mol. Boil. 247, 717-725 (1995).
20. Feher, V. A. & Cavanagh, J. Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F. Nature 400, 289-292 (1999).
21. Krebs, E. G. in The Enzymes (ed. Boyer, P. D. & Krebs, E. G.) 3rd edn Vol. 17 3-20 (Academic, New York, 1986).
22. Hurley, J. H., Dean, A. M., Thorsness, P. E., Koshland, D. E. Jr & Stroud, R. M. Regulation of isocitrate dehydrogenase by phosphorylation involves no long-range conformational change in the free enzyme. J. Biol. Chem. 265, 3599-3602 (1990).
23. Russo, A. A., Jeffrey, P. D. & Pavletich, N. P. Structural basis of cydin-dependent kinase activation by phosphorylation. Nature Struct. Biol. 3, 696-700 (1996).
24. Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H. & Goldsmith, E. J. Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell 90, 859-869 (1997).
25. Barford, D., Hu, S. H. & Johnson, L. N. Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP. J. Mol. Biol. 218, 233-260 (1991).
26. Lin, K., Rath, V. L., Dai, S. C., Fletterick, R. J. & Hwang, P. K. A protein phosphorylation switch at the conserved allosteric site in GP. Science 273, 1539-1542 (1996).
27. Altieri, A. S., Hinton, D. P. & Byrd, R. A. Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements. J. Am. Chem. Soc. 117, 7566-7567 (1995).
28. Güntert, P., Mumenthaler, C. & Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273, 283-298 (1997).
29. Koradi, R., Billeter, M. & Wüthrich, K. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55 (1996).