Crystal structure of the histidine-containing phosphotransfer protein ZmHP2 from maize

Protein Science

Volumn 14, Issue 1, 2005, Pages 202-208

  Sugawara, Hajime ^a   Kawano, Yoshiaki ^b   Hatakeyama, Tomomitsu ^c   Yamaya, Tomoyuki ^a   Kamiya, Nobuo ^b   Sakakibara, Hitoshi ^a  

^a REKEN Center for Sustainable Resource Science   (Japan)

^b RIKEN HARIMA INSTITUTE   (Japan)

^c NAGASAKI UNIVERSITY   (Japan)

Author keywords

Crystal structure; Four helix bundle; Histidine containing phosphotransfer protein; Two component system; Zea mays

Indexed keywords

ARGININE; CARRIER PROTEIN; GLUTAMIC ACID; GLUTAMINE; HISTIDINE CONTAINING PHOSPHOTRANSFER PROTEIN ZMHP2; PROTEIN HISTIDINE KINASE; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; HYDROGEN BOND; MAIZE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; STRESS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; HISTIDINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHOTRANSFERASES; PLANT PROTEINS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; ZEA MAYS;

EMBRYOPHYTA; ZEA MAYS;

EID: 11144223894     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041076905     Document Type: Article

References (56)

1. Anderson, J.W., Pullen, K., Georges, F., Klevit, R.E., and Waygood, E.B. 1993. The involvement of the arginine 17 residue in the active site of the histidine-containing protein, HPr, of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli. J. Biol. Chem. 268: 12325-12333.
2. Asakura, Y., Hagino, T., Ohta, Y., Aoki, K., Yonekura-Sakakibara, K., Deji, A., Yamaya, T., Sugiyama, T., and Sakakibara, H. 2003. Molecular characterization of His-Asp phosphorelay signaling factors in maize leaves: Implications of the signal divergence by cytokinin-inducible response regulators in the cytosol and the nuclei. Plant Mol. Biol. 52: 331-341.
3. Brandstatter, I. and Kieber, J.J. 1998. Two genes with similarity to bacterial response regulators are rapidly and specifically induced by cytokinin in Arabidopsis. Plant Cell 10: 1009-1019.
4. Brünger, A.T. 1997. Free R value: Cross-validation in crystallography. Meth. Enzymol. 277: 366-396.
5. 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., et al. 1998. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54: 905-921.
6. D'Agostino, I.B., Deruere, J., and Kieber, J.J. 2000. Characterization of the response of the Arabidopsis response regulator gene family to cytokinin. Plant Physiol. 124: 1706-1717.
7. DeLano, W.L. 2002. The PyMOL Molecular Graphics System. DeLano Scientific, San Carlos, CA, USA.
8. Garrett, D.S., Seok, Y.J., Peterkofsky, A., Gronenborn, A.M., and Clore, G.M. 1999. Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr. Nat. Struct. Biol. 6: 166-173.
9. Hendrickson, W.A., Horton, J.R., and LeMaster, D.M. 1990. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure. EMBO J. 9: 1665-1672.
10. Hua, J. and Meyerowitz, E.M. 1998. Ethylene responses are negatively regulated by a receptor gene family in Arabidopsis thaliana. Cell 94: 261-271.
11. Hutchinson, E.G. and Thornton, J.M. 1996. PROMOTIF - a program to identify and analyze structural motifs in proteins. Protein Sci. 5: 212-220.
12. Hwang, I., Chen, H.C., and Sheen, J. 2002. Two-component signal transduction pathways in Arabidopsis. Plant Physiol. 129: 500-515.
13. Ikegami, T., Okada, T., Ohki, I., Hirayama, J., Mizuno, T., and Shirakawa, M. 2001. Solution structure and dynamic character of the histidine-containing phosphotransfer domain of anaerobic sensor kinase ArcB from Escherichia coli. Biochemistry 40: 375-386.
14. Imamura, A., Hanaki, N., Nakamura, A., Suzuki, T., Taniguchi, M., Kiba, T., Ueguchi, C., Sugiyama, T., and Mizuno, T. 1999. Compilation and characterization of Arabidopsis thaliana response regulators implicated in His-Asp phosphorelay signal transduction. Plant Cell Physiol. 40: 733-742.
15. Inoue, T., Higuchi, M., Hashimoto, Y., Seki, M., Kobayashi, M., Kato, T., Tabata, S., Shinozaki, K., and Kakimoto, T. 2001. Identification of CRE1 as a cytokinin receptor from Arabidopsis. Nature 409: 1060-1063.
16. Janiak-Spens, F. and West, A.H. 2000. Functional roles of conserved amino acid residues surrounding the phosphorylatable histidine of the yeast phosphorelay protein YPD1. Mol. Microbiol. 37: 136-144.
17. Kakimoto, T. 2003. Perception and signal transduction of cytokinins. Annu. Rev. Plant Biol. 54: 605-627.
18. Kato, M., Mizuno, T., Shimizu, T., and Hakoshima, T. 1997. Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB. Cell 88: 717-723.
19. -. 1999. Refined structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli at 1.57 Å resolution. Acta Crystallogr. D Biol. Crystallogr. 55: 1842-1849.
20. Kiba, T., Taniguchi, M., Imamura, A., Ueguchi, C., Mizuno, T., and Sugiyama, T. 1999. Differential expression of genes for response regulators in response to cytokinins and nitrate in Arabidopsis thaliana. Plant Cell Physiol. 40: 767-771.
21. Kiba, T., Yamada, H., Sato, S., Kato, T., Tabata, S., Yamashino, T., and Mizuno, T. 2003. The type-A response regulator, ARR15, acts as a negative regulator in the cytokinin-mediated signal transduction in Arabidopsis thaliana. Plant Cell Physiol. 44: 868-874.
22. Kruse, R., Hengstenberg, W., Beneicke, W., and Kalbitzer, H.R. 1993. Involvement of various amino- and carboxyl-terminal residues in the active site of the histidine-containing protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus: Site-directed mutagenesis with the ptsH gene, biochemical characterization and NMR studies of the mutant proteins. Protein Eng. 6: 417-423.
23. Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26: 283-291.
24. 15N heteronuclear NMR studies of Escherichia coli thioredoxin in samples isotopically labeled by residue type. Biochemistry 24: 7263-7268.
25. Matsushika, A. and Mizuno, T. 1998a. Mutational analysis of the histidine-containing phosphotransfer (HPt) signaling domain of the ArcB sensor in Escherichia coli. Biosci. Biotechnol. Biochem. 62: 2236-2238.
26. -. 1998b. The structure and function of the histidine-containing phosphotransfer (HPt) signaling domain of the Escherichia coli ArcB sensor. J. Biochem. (Tokyo) 124: 440-445.
27. Matthews, B.W. 1968. Solvent content of protein crystals. J. Mol. Biol. 33: 491-497.
28. McRee, D.E. 1999. XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125: 156-165.
29. Miyata, S., Urao, T., Yamaguchi-Shinozaki, K., and Shinozaki, K. 1998. Characterization of genes for two-component phosphorelay mediators with a single HPt domain in Arabidopsis thaliana. FEBS Lett. 437: 11-14.
30. Mourey, L., Da Re, S., Pedelacq, J.D., Tolstykh, T., Faurie, C., Guillet, V., Stock, J.B., and Samama, J.P. 2001. Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis. J. Biol. Chem. 276: 31074-31082.
31. Murshudov, G.N., Vagin, A.A., Lebedev, A., Wilson, K.S., and Dodson, E.J. 1999. Efficient anisotropic refinement of macromolecular structures using FFT. Acta Crystallogr. D Biol. Crystallogr. 55: 247-255.
32. Navaza, J. 1994. AMoRe: An automated package for molecular replacement. Acta Crystallogr. A 50: 157-163.
33. Otwinowski, Z. and Minor, W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Meth. Enzymol. 276: 307-326.
34. Papon, N., Oudin, A., Clastre, M., Rideau, M., Chénieux, J.-C., and Crèche, J. 2002. Isolation of CrHPt1, a cDNA encoding a histidine-containing phospho-transfer domain in Catharanthus roseus. Acta Bot. Gallica 149: 67-77.
35. Pischke, M.S., Jones, L.G., Otsuga, D., Fernandez, D.E., Drews, G.N., and Sussman, M.R. 2002. An Arabidopsis histidine kinase is essential for mega-gametogenesis. Proc. Natl. Acad. Sci. 99: 15800-15805.
36. Riechmann, J.L., Heard, J., Manin, G., Reuber, L., Jiang, C., Keddie, J., Adam, L., Pineda, O., Ratcliffe, O.J., Samaha, R.R., et al. 2000. Arabidopsis transcription factors: Genome-wide comparative analysis among eukaryotes. Science 290: 2105-2110.
37. Saito, H. 2001. Histidine phosphorylation and two-component signaling in eukaryotic cells. Chem. Rev. 101: 2497-2509.
38. Sakakibara, H., Suzuki, M., Takei, K., Deji, A., Taniguchi, M., and Sugiyama, T. 1998. A response-regulator homologue possibly involved in nitrogen signal transduction mediated by cytokinin in maize. Plant J. 14: 337-344.
39. Sakakibara, H., Hayakawa, A., Deji, A., Gawronski, S.W., and Sugiyama, T. 1999. His-Asp phosphotransfer possibly involved in the nitrogen signal transduction mediated by cytokinin in maize: Molecular cloning of cDNAs for two-component regulatory factors and demonstration of phosphotransfer activity in vitro. Plant Mol. Biol. 41: 563-573.
40. Song, H.K., Lee, J.Y., Lee, M.G., Moon, J., Min, K., Yang, J.K., and Suh, S.W. 1999. Insights into eukaryotic multistep phosphorelay signal transduction revealed by the crystal structure of Ypd1p from Saccharomyces cerevisiae. J. Mol. Biol. 293: 753-761.
41. Stock, A.M., Robinson, V.L., and Goudreau, P.N. 2000. Two-component signal transduction. Annu. Rev. Biochem. 69: 183-215.
42. Suzuki, T., Imamura, A., Ueguchi, C., and Mizuno, T. 1998. Histidine-containing phosphotransfer (HPt) signal transducers implicated in His-to-Asp phosphorelay in Arabidopsis. Plant Cell Physiol 39: 1258-1268.
43. Suzuki, T., Sakurai, K., Imamura, A., Nakamura, A., Ueguchi, C., and Mizuno, T. 2000. Compilation and characterization of histidine-containing phosphotransmitters implicated in His-to-Asp phosphorelay in plants: AHP signal transducers of Arabidopsis thaliana. Biosci. Biotechnol. Biochem. 64: 2486-2489.
44. Suzuki, T., Sakurai, K., Ueguchi, C., and Mizuno, T. 2001. Two types of putative nuclear factors that physically interact with histidine-containing phosphotransfer (Hpt) domains, signaling mediators in His-to-Asp phosphorelay, in Arabidopsis thaliana. Plant Cell Physiol. 42: 37-45.
45. Taniguchi, M., Kiba, T., Sakakibara, H., Ueguchi, C., Mizuno, T., and Sugiyama, T. 1998. Expression of Arabidopsis response regulator homologs is induced by cytokinins and nitrate. FEBS Lett. 429: 259-262.
46. Terwilliger, T.C. 2000. Maximum-likelihood density modification. Acta Crystallogr. D Biol. Crystallogr. 56: 965-972.
47. Terwilliger, T.C. and Berendzen, J. 1999. Automated MAD and MIR structure solution. Acta Crystallogr. D Biol. Crystallogr. 55: 849-861.
48. To, J.P., Haberer, G., Ferreira, F.J., Deruere, J., Mason, M.G., Schaller, G.E., Alonso, J.M., Ecker, J.R., and Kieber, J.J. 2004. Type-A Arabidopsis response regulators are partially redundant negative regulators of cytokinin signaling. Plant Cell 16: 658-671.
49. Urao, T., Yakubov, B., Satoh, R., Yamaguchi-Shinozaki, K., Seki, M., Hirayama, T., and Shinozaki, K. 1999. A transmembrane hybrid-type histidine kinase in Arabidopsis functions as an osmosensor. Plant Cell 11: 1743-1754.
50. glucose of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system. EMBO J. 19: 5635-5649.
51. Winn, M.D., Isupov, M.N., and Murshudov, G.N. 2001. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D Biol. Crystallogr. 57: 122-133.
52. Xu, Q. and West, A.H. 1999. Conservation of structure and function among histidine-containing phosphotransfer (HPt) domains as revealed by the crystal structure of YPD1. J. Mol. Biol. 292: 1039-1050.
53. Xu, Q., Porter, S.W., and West, A.H. 2003. The yeast YPD1/SLN1 complex: Insights into molecular recognition in two-component signaling systems. Structure 11: 1569-1581.
54. Yamada, H., Suzuki, T., Terada, K., Takei, K., Ishikawa, K., Miwa, K., Yamashino, T., and Mizuno, T. 2001. The Arabidopsis AHK4 histidine kinase is a cytokinin-binding receptor that transduces cytokinin signals across the membrane. Plant Cell Physiol. 42: 1017-1023.
55. Yamamoto, M., Kumasaka, T., Fujisawa, T., and Ueki, T. 1998. Trichromatic concept at SPring-8 RIKEN beamline I. J. Synchrotron Radiat. 5: 222-225.
56. Yonekura-Sakakibara, K., Kojima, M., Yamaya, T., and Sakakibara, H. 2004. Molecular characterization of cytokinin-responsive histidine kinases in maize. Differential ligand preferences and response to cis-zeatin. Plant Physiol. 134: 1654-1661.