Switched or not?: The structure of unphosphorylated CheY bound to the N terminus of FliM

Journal of Bacteriology

Volumn 188, Issue 21, 2006, Pages 7354-7363

  Dyer, Collin M ^a   Dahlquist, Frederick W ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MAGNESIUM; MOLECULAR MOTOR; PROTEIN CHEY; PROTEIN FLIM; REGULATOR PROTEIN; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

ALLOSTERISM; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; COMPLEX FORMATION; CRYSTALLOGRAPHY; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TARGETING;

ALLOSTERIC REGULATION; BACTERIAL PROTEINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; MEMBRANE PROTEINS; MODELS, MOLECULAR; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SIGNAL TRANSDUCTION; THREONINE;

ESCHERICHIA COLI;

EID: 33750435591     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00637-06     Document Type: Article

References (28)

1. Ames, S. K., N. Frankeema, and L. J. Kenney. 1999. C-terminal DNA binding stimulates N-terminal phosphorylation of the outer membrane protein regulator OmpR from Escherichia coli. Proc. Natl. Acad. Sci. USA 96:11792-11797.
2. Appleby, J., and R. Bourret. 1998. Proposed signal transduction role for conserved CheY residue Thr87, a member of the response regulator active-site quintet. J. Bacteriol. 180:3563-3569.
3. Barak, R., and M. Eisenbach. 1992. Correlation between phosphorylation of the chemotaxis protein CheY and its activity at the flagellar motor. Biochemistry 31:1821-1826.
4. Bellsolell, L., J. Prieto, L. Serrano, and M. Coll. 1994. Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface. J. Mol. Biol. 238:489-495.
5. Brunger, A. T., P. D. Adams, G. M. Clore, W. L. DeLano, P. Gros, R. W. Grosse-Kunstleve, J.-S. Jiang, J. Kuszewski, N. Nilges, N. S. Pannu, R. J. Read, L. M. Rice, T. Simonson, and G. L. Warren. 1998. Crystallography and NMR systems (CNS): a new software system for macromolecular structure determination. Acta Crystallogr. D 54:905-921.
6. Clegg, D. O., and D. E. J. Koshland. 1984. The role of a signaling protein in bacterial sensing: behavioral effects of increased gene expression. Proc. Natl. Acad. Sci. USA 81:5056-5060.
7. Collaborative Computational Project. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50:760-763.
8. D13KYD6W alone and in complex with a FliM peptide. J. Mol. Biol. 342:1325-1335.
9. Feher, V. A., and J. Cavanagh. 1999. Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F. Nature 400:289-293.
10. Formaneck, M., L. Ma, and Q. Cui. 2006. Reconciling the "old" and "new" views of protein allostery: a molecular simulation study of chemotaxis Y protein (CheY). Proteins 63:846-867.
11. Guhaniyogi, J., V. L. Robinson, and A. M. Stock. 2006. Crystal structures of beryllium fluoride-free and beryllium bound-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation. J. Mol. Biol. 359:624-645.
12. Halkides, C. J., M. M. McEvoy, E. Casper, P. Matsumura, K. Volz, and F. W. Dahlquist. 2000. The 1.9 Å resolution crystal structure of phosphono-Che Y, an analogue of the active form of the response regulator, CheY. Biochemistry 39:5280-5286.
13. Hess, J. F., R. B. Bourret, and M. I. Simon. 1991. Phosphorylation assays for proteins of the two-component regulatory system controlling chemotaxis in Escherichia coli. Methods Enzymol. 200:188-204.
14. Jiang, M., R. B. Bourret, M. I. Simon, and K. Volz. 1997. Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.3 A structure of an aspartate to lysine mutant at position 13 of CheY. J. Biol. Chem. 272:11850-11855.
15. Jones, T. A., J.-Y. Zou, S. W. Cowan, and M. Kjeldgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47:110-119.
16. Kabsch, W. 1976. A solution for the best rotation to relate two sets of vectors. Acta Crystallogr. A 32:922-923.
17. Kissinger, C. R., D. K. Gehlhaar, and D. B. Fogel. 1999. Rapid automated molecular replacement by evolutionary search. Acta Crystallogr. D 55:484-491.
18. Lakowski, R. A., M. W. Macarthur, D. S. Moss, and J. M. Thornton. 1993. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:283-291.
19. Lee, S.-Y., H. S. Clio, J. G. Pelton, D. Van, E. A. Berry, and D. E. Wemmer. 2001. Crystal structure of activated CheY. J. Biol. Chem. 276:16425-16431.
20. Lee, S.-Y., H. S. Cho, J. G. Pelton, D. Van, R. K. Henderson, D. S. King, L.-s. Huang, S. Kustu, E. A. Berry, and D. E. Wemmer. 2001. Crystal structure of an activated response regulator hound to its target. Nat. Struct. Biol. 8:52-56.
21. Leslie, A. G. W. 1992. Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 + ESF-EAMCB newsletter on protein crystallography, no. 26. Daresbury Laboratories, Warrington, United Kingdom.
22. McEvoy, M., A. C. Hausrath, G. B. Randolph, S. J. Remington, and F. W. Dahlquist. 1998. Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway. Proc. Natl. Acad. Sci. USA 95:7333-7338.
23. 15N) NMR spectroscopy. Biochemistry 33:10731-10742.
24. Schuster, M., R. E. Silversmith, and R. B. Bourret. 2001. Conformational coupling in the chemotaxis response regulator CheY. Proc. Natl. Acad. Sci. USA 98:6003-6008.
25. Simonovic, M., and K. Volz. 2001. A distinct meta-active conformation in the 1.1-Å resolution structure of wild-type apo CheY. J. Biol. Chem. 276:28637-28640.
26. Stock, A., E. Martinez-Hackert, B. Rasmussen, A. West, J. Stock, D. Ringe, and G. Petsko. 1993. Structure of the Mg(2+) hound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis. Biochemistry 32:13375-13380.
27. Volkman, B. F., D. Lipson, D. E. Wemmer, and D. Kern. 2001. Two-state allosteric behavior in a single-domain signaling protein. Science 291:2429-2433.
28. Volz, K., and P. Matsumura. 1991. Crystal structure of Escherichia coli refined at 1.7-Å resolution. J. Biol. Chem. 266:15511-15519.