Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumoniae

Journal of Molecular Biology

Volumn 326, Issue 4, 2003, Pages 1203-1217

  Allen, Gregory S ^a   Steinhauer, Katrin ^b   Hillen, Wolfgang ^b   Stülke, Jörg ^b   Brennan, Richard G ^a  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^b UNIVERSITY OF ERLANGEN NUREMBERG   (Germany)

Author keywords

Catabolite repression; HPr kinase; Mycoplasma pneumoniae; Ser Thr kinase, Ser Thr phosphatase

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID; BACTERIAL ENZYME; PHOSPHATASE; PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP); PROTEIN HISTIDINE KINASE; PROTEIN SUBUNIT; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLMURAMOYL ALANYL DEXTRO GLUTAMATE:MESO DIAMINOPIMELATE LIGASE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME STRUCTURE; ESCHERICHIA COLI; GENE MUTATION; LACTOBACILLUS CASEI; MYCOPLASMA PNEUMONIAE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; STAPHYLOCOCCUS XYLOSUS; STRUCTURE ANALYSIS;

ESCHERICHIA COLI; FIRMICUTES; HOMO; LACTOBACILLUS; LACTOBACILLUS CASEI; MYCOPLASMA; MYCOPLASMA PNEUMONIAE; POSIBACTERIA; STAPHYLOCOCCUS; STAPHYLOCOCCUS XYLOSUS;

EID: 0037470605     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01378-5     Document Type: Article

References (43)

1. Fieulaine S., Morera S., Poncet S., Monedero V., Gueguen-Chaignon V., Galinier A., et al. X-ray structure of HPr kinase: a bacterial protein kinase with a P-loop nucleotide-binding domain. EMBO J. 20:2001;3917-3927.
2. Deutscher J., Galinier A., Martin-Verstraete I. Carbohydrate uptake and metabolism. Sonenshein A.L., Hoch J.A., Losick R. Bacillus subtilis and its Closest Relatives: From Genes to Cells. 2002;129-150 ASM Press, Washington, DC.
3. Saier M.H. Jr, Ramseier T.M. The catabolite repressor/activator (Cra) protein of enteric bacteria. J. Bacteriol. 178:1996;3411-3417.
4. Stülke J., Hillen W. Regulation of carbon catabolism in Bacillus species. Annu. Rev. Microbiol. 54:2000;849-880.
5. Fujita Y., Freese E. Purification and properties of fructose-1,6-bisphosphatase of Bacillus subtilis. J. Biol. Chem. 254:1979;5340-5349.
6. Deutscher J., Kessler U., Hengstenberg W. Streptococcal phosphoenolpyruvate: sugar phosphotransferase system: purification and characterization of a phosphoprotein phosphatase which hydrolyzes the phosphoryl bond in seryl-phosphorylated histidine-containing protein. J. Bacteriol. 163:1985;1203-1209.
7. Hueck C.J., Hillen W., Saier M.H. Jr. Analysis of a cis-active sequence mediating catabolite repression in Gram-positive bacteria. Res. Microbiol. 145:1994;503-518.
8. Tobisch S., Zühlke D., Bernhardt J., Stülke J., Hecker M. Role of CcpA in regulation of the central pathways of carbon catabolism in Bacillus subtilis. J. Bacteriol. 181:1999;6996-7004.
9. Yoshida K., Kobayashi K., Miwa Y., Kang C.M., Matsunaga M., Yamaguchi H., et al. Combined transcriptome and proteome analysis as a powerful approach to study genes under glucose repression in Bacillus subtilis. Nucl. Acids Res. 29:2001;683-692.
10. Moreno M.S., Schneider B.L., Maile R.R., Weyler W., Saier M.H. Catabolite repression mediated by the CcpA protein in Bacillus subtilis: novel modes of regulation revealed by whole-genome analyses. Mol. Microbiol. 39:2001;1366-1381.
11. Henkin T.M., Grundy F.J., Nicholson W.L., Chambliss G.H. Catabolite repression of alpha-amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacl and galR repressors. Mol. Microbiol. 5:1991;575-584.
12. Weickert M.J., Adhya S. A family of bacterial regulators homologous to Gal and Lac repressors. J. Biol. Chem. 267:1992;15869-15874.
13. Kim J.H., Guvener Z.T., Cho J.Y., Chung K.C., Chambliss G.H. Specificity of DNA binding activity of the Bacillus subtilis catabolite control protein CcpA. J. Bacteriol. 177:1995;5129-5134.
14. Weickert M.J., Chambliss G.H. Site-directed mutagenesis of a catabolite repression operator sequence in Bacillus subtilis. Proc. Natl Acad. Sci. USA. 87:1990;6238-6242.
15. Deutscher J., Küster E., Bergstedt U., Charrier V., Hillen W. Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram-positive bacteria. Mol. Microbiol. 15:1995;1049-1053.
16. Galinier A., Deutscher J., Martin-Verstraete I. Phosphorylation of either Crh or HPr mediates binding of CcpA to the Bacillus subtilis xyn cre and catabolite repression of the xyn operon. J. Mol. Biol. 286:1999;307-314.
17. Jault J.M., Fieulaine S., Nessler S., Gonzalo P., Di Pietro A., Deutscher J., Galinier A. The HPr kinase from Bacillus subtilis is a homo-oligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding. J. Biol. Chem. 275:2000;1773-1780.
18. Steinhauer K., Jepp T., Hillen W., Stülke J. A novel mode of control of Mycoplasma pneumoniae HPr kinase/phosphatase activity reflects its parasitic lifestyle. Microbiology. 148:2002;3277-3284.
19. Hutchison C.A., Peterson S.N., Gill S.R., Cline R.T., White O., Fraser C.M., et al. Global transposon mutagenesis and a minimal Mycoplasma genome. Science. 286:1999;2165-2169.
20. Marquez J.A., Hasenbein S., Koch B., Fieulaine S., Nessler S., Russell R.B., et al. Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 Å resolution: mimicking the product/substrate of the phospho transfer reactions. Proc. Natl Acad. Sci. USA. 99:2002;3458-3463.
21. Russell R.B., Marquez J.A., Hengstenberg W., Scheffzek K. Evolutionary relationship between the bacterial HPr kinase and the ubiquitous PEP-carboxykinase: expanding the P-loop nucleotidyl transferase superfamily. FEBS Letters. 517:2002;1-6.
22. Gordon E., Flouret B., Chantalat L., van Heijenoort J., Mengin-Lecreulx D., Dideberg O. Crystal structure of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate: meso-diaminopimelate ligase from Escherichia coli. J. Biol. Chem. 276:2001;10999-11006.
23. Reizer J., Hoischen C., Titgemeyer F., Rivolta C., Rabus R., Stülke J., et al. A novel protein kinase that controls carbon catabolite repression in bacteria. Mol. Microbiol. 27:1998;1157-1169.
24. Hanson K.G., Steinhauer K., Reizer J., Hillen W., Stülke J. HPr kinase/phosphatase of Bacillus subtilis: expression of the gene and effects of mutations on enzyme activity, growth and carbon catabolite repression. Microbiology. 148:2002;1805-1811.
25. Kravanja M., Engelmann R., Dossonnet V., Blüggel M., Meyer H.E., Frank R., et al. The hprK gene of Enterococcus faecalis encodes a novel bifunctional enzyme: the HPr kinase/phosphatase. Mol. Microbiol. 31:1999;59-66.
26. Steinhauer K., Allen G.S., Hillen W., Stülke J., Brennan R.G. Crystallization, preliminary X-ray analysis and biophysical characterization of HPr kinase/phosphatase of Mycoplasma pneumoniae. Acta Crystallog. sect. D Biol. Crystallog. 58:2002;515-518.
27. Aurora R., Rose G.D. Helix capping. Protein Sci. 7:1998;21-38.
28. Holm L., Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20:1995;478-480.
29. Kleywegt G.J. Experimental assessment of differences between related protein crystal structures. Acta Crystallog. sect. D Biol. Crystallog. 55:1999;1878-1884.
30. Traut T.W. The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide-binding sites. Eur. J. Biochem. 222:1994;9-19.
31. Matte A., Tari L.W., Goldie H., Delbaere L.T. Structure and mechanism of phosphoenolpyruvate carboxykinase. J. Biol. Chem. 272:1997;8105-8108.
32. Shirakihara Y., Evans P.R. Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products. J. Mol. Biol. 204:1988;973-994.
33. Galinier A., Lavergne J.P., Geourjon C., Fieulaine S., Nessler S., Jault J.M. A new family of phosphotransferases with a P-loop motif. J. Biol. Chem. 277:2002;11362-11367.
34. Zhang Z.Y., Wang Y., Wu L., Fauman E.B., Stuckey J.A., Schubert H.L., et al. The Cys(X)5Arg catalytic motif in phosphoester hydrolysis. Biochemistry. 33:1994;15266-15270.
35. Jackson M.D., Denu J.M. Molecular reactions of protein phosphatases-insights from structure and chemistry. Chem. Rev. 101:2001;2313-2340.
36. Pflugrath J.W. The finer things in X-ray diffraction data collection. Acta Crystallog. sect. D Biol. Crystallog. 55:1999;1718-1725.
37. Terwilliger T.C., Berendzen J. Automated MAD and MIR structure solution. Acta Crystallog. sect. D Biol. Crystallog. 55:1999;849-861.
38. Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallog. sect. D Biol. Crystallog. 56:2000;965-972.
39. McRee D.E. XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125:1999;156-165.
40. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallog. sect. D Biol. Crystallog. 54:1998;905-921.
41. Peitsch M.C., Wells T.N., Stampf D.R., Sussman J.L. The Swiss-3DImage collection and PDB-Browser on the World-Wide Web. Trends Biochem. Sci. 20:1995;82-84.
42. Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
43. Barton G.J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40.