Structure and function of an unusual family of protein phosphatases: The bacterial chemotaxis proteins CheC and CheX

Molecular Cell

Volumn 16, Issue 4, 2004, Pages 563-574

  Park, Sang Youn ^a   Chao, Xingjuan ^a   Gonzalez Bonet, Gabriela ^a   Beel, Bryan D ^a   Bilwes, Alexandrine M ^a   Crane, Brian R ^a  

^a Department of Obstetrics Gynecology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHEC PROTEIN; CHED PROTEIN; CHEX PROTEIN; PHOSPHATASE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIUM; BETA SHEET; BINDING AFFINITY; CHEMOTAXIS; CONTROLLED STUDY; CORRELATION ANALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ESCHERICHIA COLI; MOLECULAR EVOLUTION; MUTATIONAL ANALYSIS; NONHUMAN; PROTEIN DEPHOSPHORYLATION; PROTEIN FAMILY; PROTEIN FUNCTION; STRUCTURE ANALYSIS; TREPANOMA MARITIMA;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACILLUS SUBTILIS; BACTERIAL PROTEINS; BINDING SITES; CHEMOTAXIS; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ESCHERICHIA COLI; FLAGELLA; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHORUS RADIOISOTOPES; PHOSPHORYLATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE; TREPONEMA;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 8844239143     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.10.018     Document Type: Article

References (49)

1. Alon U., Surette M.G., Barkai N., Liebler S. Robustness in bacterial chemotaxis. Nature. 397:1999;168-171
2. Aravind L., Galperin M.Y., Koonin E.V. The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold. Trends Biochem. Sci. 23:1998;127-129
3. Bilwes A.M., Quezada C.M., Croal L.R., Crane B.R., Simon M.I. Nucleotide binding by the histidine kinase CheA. Nat. Struct. Biol. 8:2001;353-360
4. Bischoff D.S., Ordal G.W. Identification and characterization of FliY, a novel component of the Bacillus subtilis flagellar switch complex. Mol. Microbiol. 6:1992;2715-2723
5. Blair D.F. How bacteria sense and swim. Annu. Rev. Microbiol. 49:1995;489-522
6. Bren A., Eisenbach M. The N terminus of the flagellar switch protein, FliM, is the binding domain for the chemotactic response regulator, CheY. J. Mol. Biol. 278:1998;507-514
7. Brunger 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., et al. Crystallography and NMR system. a new software suite for macromolecular structure determination Acta Crystallogr. D Biol. Crystallogr. 54:1998;905-921
8. CCP4 Collaborative Computational Project, Number 4) The CCP4 suite. programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50:1994;760-763
9. Cho H., Wang W., Kim R., Yokota H., Damo S., Kim S.H., Wemmer D., Kustu S., Yan D. BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate. structure of a BeF(3)(-) complex with phosphoserine phosphatase Proc. Natl. Acad. Sci. USA. 98:2001;8525-8530
10. Cronet P., Bellsolell L., Sander C., Coll M., Serrano L. Investigating the structural determinants of the p21-like triphosphate and Mg2+ binding site. J. Mol. Biol. 249:1995;654-664
11. Esnouf R.M. An extensively modified version of Molscript that includes greatly enhanced coloring capabilities. J. Mol. Graph. 15:1997;133-138
12. Falke J.J., Bass R.B., Butler S.L., Chervitz S.A., Danielson M.A. The two-component signaling pathway of bacterial chemotaxis. a molecular view of signal transduction by receptors, kinases, and adapation enzymes Annu. Rev. Cell Dev. Biol. 13:1997;457-512
13. Fuhrer D.K., Ordal G.W. Bacillus subtilis CheN, a homolog of CheA, the central regulator of chemotaxis in Escherichia coli. J. Bacteriol. 173:1991;7443-7448
14. Garrity L.F., Ordal G.W. Chemotaxis in Bacillus subtilis. how bacteria monitor environmental signals Pharmacol. Ther. 68:1995;87-104
15. Hess J.F., Oosawa K., Kaplan N., Simon M.I. Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis. Cell. 53:1988;79-87
16. Holm L., Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233:1993;123-138
17. Jackson M.D., Denu J.M. Molecular reactions of protein phosphatases. insights from structure and chemistry Chem. Rev. 101:2001;2313-2340
18. Kirby J.R., Kristich C.J., Saulmon M.M., Zimmer M.A., Garrity L.F., Zhulin I.B., Ordal G.W. CheC is related to the family of flagellar switch proteins and acts independently from CheD to control chemotaxis in Bacillus subtilis. Mol. Microbiol. 42:2001;573-585
19. Kolmosin K., Aqvist J. The catalytic mechanism of protein tyrosine phosphatases revisited. FEBS Lett. 498:2001;208-213
20. Kraulis P.J. Molscript. a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24:1991;946-950
21. Kristich C.J., Ordal G.W. Bacillus subtilis CheD is a chemoreceptor modification enzyme required for chemotaxis. J. Biol. Chem. 277:2002;25356-25362
22. Lee S.Y., Cho H.S., Pelton J.G., Yan D.L., Berry E.A., Wemmer D.E. Crystal structure of activated CheY. comparison with other activated receiver domains J. Biol. Chem. 276:2001;16425-16431. a
23. Lee S.Y., Cho H.S., Pelton J.G., Yan D.L., Henderson R.K., King D.S., Huang L.S., Kustu S., Berry E.A., Wemmer D.E. Crystal structure of an activated response regulator bound to its target. Nat. Struct. Biol. 8:2001;52-56. b
24. Lowy D.R., Willumsen B.M. Function and regulation of ras. Annu. Rev. Biochem. 62:1993;851-891
25. Maegley K.A., Admiraal S.J., Herschlag D. Ras-catalyzed hydrolysis of GTP. a new perspective from model studies Proc. Natl. Acad. Sci. USA. 93:1996;8160-8166
26. Mathews M.A., Tang H.L., Blair D.F. Domain analysis of the FliM protein of Escherichia coli. J. Bacteriol. 180:1998;5580-5590
27. McRee D.E. XtalView. a visual protein crystallographic software system for X11/Xview J. Mol. Graph. 10:1992;44-47
28. Merritt E.A., Murphy M.E.P. Raster3D Version 2.0. a program for photorealistic molecular graphics Acta Crystallogr. D Biol. Crystallogr. 50:1994;869-873
29. Navaza J. AMoRe. an automated package for molecular replacement Acta Crystallogr. A. 50:1994;157-163
30. Nelson K.E., Eisen J.A., Fraser C.M. Genome of Thermotoga maritima MSB8. Methods Enzymol. 330:2001;169-180
31. Otwinowski A., Minor W. Processing of X-ray diffraction data in oscillation mode. Methods Enzymol. 276:1997;307-325
32. Pannifer A.D.B., Flint A.J., Tonks N.K., Barford D. Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by X-ray crystallography. J. Biol. Chem. 273:1988;10454-10462
33. Parkinson J.S., Kofoid E.C. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26:1992;71-112
34. Rosario M.M., Ordal G.W. CheC and CheD interact to regulate methylation of Bacillus subtilis methyl-accepting chemotaxis proteins. Mol. Microbiol. 21:1996;511-518
35. Rosario M.M., Kirby J.R., Bochar D.A., Ordal G.W. Chemotactic methylation and behavior in Bacillus subtilis. role of two unique proteins, CheC and CheD Biochemistry. 34:1995;3823-3831
36. Saulmon M.M., Karatan E., Ordal G.W. Effect of loss of CheC and other adaptational proteins on chemotactic behaviour in Bacillus subtilis. Microbiol. 150:2004;581-589
37. Scheffzek K., Ahmadian M.R., Kabsch W., Wiesmuller L., Lautwein A., Schmitz F., Wittinghofer A. The Ras-RasGAP complex. structural basis for GTPase activation and its loss in oncogenic Ras mutants Science. 277:1997;333-338
38. Silversmith R.E., Guanga G.P., Betts L., Chu C., Zhao R., Bourret R.B. CheZ-mediated dephosphorylation of the Escherichia coli chemotaxis response regulator CheY. role for CheY glutamate 89 J. Bacteriol. 185:2003;1495-1502
39. Sourjik V., Berg H.C. Receptor sensitivity in bacterial chemotaxis. Proc. Natl. Acad. Sci. USA. 99:2002;123-127
40. Szurmant H., Ordal G.W. Diversity in chemotaxis mechanisms among the bacteria and archaea. Microbiol. Mol. Biol. Rev. 68:2004;301-319
41. Szurmant H., Bunn M.W., Cannistraro V.J., Ordal G.W. Bacillus subtilis hydrolyzes CheY-P at the location of its action, the flagellar switch. J. Biol. Chem. 278:2003;48611-48616
42. Szurmant H., Muff T.J., Ordal G.W. Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-hydrolyzing proteins in the chemotactic signal transduction cascade. J. Biol. Chem. 279:2004;21787-21792
43. Varughese K.I. Molecular recognition of bacterial phosphorelay proteins. Curr. Opin. Microbiol. 5:2002;142-148
44. Wang W., Cho H.S., Kim R., Jancarik J., Yokota H., Nguyen H.H., Grigoriev I.V., Wemmer D.E., Kim S.H. Structural characterization of the reaction pathway in phosphoserine phosphatase. crystallographic "snapshots" of intermediate states J. Mol. Biol. 319:2002;421-431
45. Wolanin P.M., Webre D.J., Stock J.B. Mechanism of phosphatase activity in the chemotaxis response regulator CheY. Biochemistry. 42:2003;14075-14082
46. Xu Q., Porter S.W., West A.H. The yeast YPD1/SLN1 complex. insights into molecular recognition in two-component signaling systems Structure (Camb). 11:2003;1569-1581
47. Zhao Y., Wu L., Noh S.J., Guan K., Zhang Z. Altering the nucleophile specificity of a protein-tyrosine phosphatase-catalyzed reaction. J. Biol. Chem. 273:1988;5484-5494
48. Zhao R., Collins E.J., Bourret R.B., Silversmith R.E. Structure and catalytic mechanism of the E. coli chernotaxis phosphatase CheZ. Nat. Struct. Biol. 9:2002;570-575
49. Zimmer M.A., Tiu J., Collins M.A., Ordal G.W. Selective methylation changes on the Bacillus subtilis chemotaxis receptor McpB promote adaptation. J. Biol. Chem. 275:2000;24264-24272