The structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY help to explain their binding affinities to the FliM and CheZ peptides

Archives of Biochemistry and Biophysics

Volumn 479, Issue 2, 2008, Pages 105-113

  McAdams, Kenneth ^a   Casper, Eric S ^a   Matthew Haas, R ^a   Santarsiero, Bernard D ^b   Eggler, Aimee L ^b   Mesecar, Andrew ^b   Halkides, Christopher J ^a  

^a UNIVERSITY OF NORTH CAROLINA WILMINGTON   (United States)

^b UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

Calorimetry; Chemical modification; Chemotaxis; Crystallography; Fluorescence; Protein phosphorylation; Structure function studies; Two component systems

Indexed keywords

CHEY PROTEIN; CHEZ ENZYME; FLAGELLAR SWITCH PROTEIN M; MOLECULAR MOTOR; MUTANT PROTEIN; PHOSPHATASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN METHYLATION; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BINDING SITES; CHEMOTAXIS; ESCHERICHIA COLI; MEMBRANE PROTEINS; MUTATION, MISSENSE; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 54249141377     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2008.08.019     Document Type: Article

References (42)

1. Matsumura P., Rydel J.J., Linzmeier R., and Vacante D. J. Bacteriol. 160 (1984) 36-41
2. Baker M.D., Wolanin P.M., and Stock J.B. BioEssays 28 (2006) 9-22
3. Silversmith R.E. Biochemistry 44 (2005) 7768-7776
4. Zhu X., Rebello J., Matsumura P., and Volz K. J. Biol. Chem. 272 (1997) 5000-5006
5. Lukat G.S., Stock A.M., and Stock J.B. Biochemistry 29 (1990) 5436-5442
6. Lee S.-Y., Cho H.S., Pelton J.G., Yan D., Berry E.A., and Wemmer D.E. J. Biol. Chem. 276 (2001) 16425-16431
7. Zhu X., Volz K., and Matsumura P. J. Biol. Chem. 272 (1997) 23758-23764
8. Volz K. Biochemistry 32 (1993) 11741-11753
9. Zhu X., Amsler C.D., Volz K., and Matsumura P. J. Bacteriol. 178 (1996) 4208-4215
10. Ganguli S., Wang H., Matsumura P., and Volz K. J. Biol. Chem. 270 (1995) 17386-17393
11. Volz K., and Matsumura P. J. Biol. Chem. 266 (1991) 15511-15519
12. Roman S.J., Meyers M., Volz K., and Matsumura P. J. Bacteriol. 174 (1992) 6247-6255
13. Lee S.-Y., Cho H.S., Pelton J.G., Yan D., Henderson R.K., King D.S., Huang L.-S., Kustu S., Berry E.A., and Wemmer D.E. Nat. Struct. Biol. 8 (2001) 52-56
14. Dyer C.M., and Dahlquist F.W. J. Bacteriol. 188 (2006) 7354-7363
15. Stock A.M., and Guhaniyogi J. J. Bacteriol. 188 (2006) 7328-7330
16. Lowry D.F., Roth A.F., Rupert P.B., Dahlquist F.W., Moy F.J., Domaille P.J., and Matsumura P. J. Biol. Chem. 269 (1994) 26358-26362
17. Hess J.F., Oosawa K., Kaplan N., and Simon M.I. Cell 53 (1988) 79-87
18. Wemmer D.E., and Kern D. J. Bacteriol. 187 (2005) 8229-8230
19. Barak R., and Eisenbach M. Biochemistry 31 (1992) 1821-1826
20. Halkides C.J., Zhu X., Phillion D.P., Matsumura P., and Dahlquist F.W. Biochemistry 37 (1998) 13674-13680
21. Halkides C.J., Bottone C.J., Casper E.S., Haas R.M., and McAdams K. Methods Enzymol. 422 (2007) 338-351
22. Bren A., and Eisenbach M. J. Mol. Biol. 278 (1998) 507-514
23. Blat Y., and Eisenbach M. Biochemistry 35 (1996) 5679-5683
24. McEvoy M.M., Bren A., Eisenbach M., and Dahlquist F.W. J. Mol. Biol. 289 (1999) 1423-1433
25. Otwinowski Z., Minor W., and Carter Jr. C.W. Methods Enzymol. 276 (1997) 307-326
26. Halkides C.J., McEvoy M.M., Casper E., Matsumura P., Volz K., and Dahlquist F.W. Biochemistry 39 (2000) 5280-5286
27. Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.-S., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., and Warren G.L. Acta Crystallogr. D Biol. Crystallogr. 54 (1998) 905-921
28. Lovell S.C., Davis I.W., Arendall III W.B., Bakker P.I.W.d., Word J.M., Prisant M.G., Richardson J.S., and Richardson D.C. Proteins Struct. Funct. Genet. 50 (2003) 437-450
29. Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. J. Appl. Crystallogr. 26 (1993) 283-291
30. Vriend G. J. Mol. Graphics 8 (1990) 52-56
31. Turnbull W.B., and Daranas A.H. J. Am. Chem. Soc. 125 (2003) 14859-14866
32. Needham J.V., Chen T.Y., and Falke J.J. Biochemistry 32 (1993) 3363-3367
33. Eftink M.R. Methods Enzymol. 278 (1997) 221-257
34. Simonovic M., and Volz K. J. Biol. Chem. 276 (2001) 28637-28640
35. Guhaniyogi J., Robinson V., and Stock A. J. Mol. Biol. 359 (2006) 624-645
36. Birck C., Mourey L., Gouet P., Fabry B., Schumacher J., Rousseau P., Kahn D., and Samama J.-P. Structure 7 (1999) 1505-1515
37. Welch M., Oosawa K., Aizawa S.-I., and Eisenbach M. Biochemistry 33 (1994) 10470-10476
38. Dyer C.M., Quillin M.L., Campos A., Lu J., McEvoy M.M., Hausrath A.C., Westbrook E.M., Matsumura P., Matthews B.W., and Dahlquist F.M. J. Mol. Biol. 342 (2004) 1325-1335
39. Appleby J.L., and Bourret R.B. J. Bacteriol. 180 (1998) 3563-3569
40. Silversmith R.E., Guanga G.P., Betts L., Chu C., Zhao R., and Bourret R.B. J. Bacteriol. 185 (2003) 1495-1502
41. Cho H.S., Lee S.-Y., Yan D., Pan X., Parkinson J.S., Kustu S., Wemmer D.E., and Pelton J.G. J. Mol. Biol. 297 (2000) 543-551
42. Mesecar A.D., Stoddard B.L., and Koshland Jr. D.E. Science 277 (1997) 202-206