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Volumn 44, Issue 4, 2005, Pages 1136-1144

Crystal structures of pyruvate phosphate dikinase from maize revealed an alternative conformation in the swiveling-domain motion

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; CATALYSIS; CRYSTAL STRUCTURE; PHOSPHATES;

EID: 13444291928     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0484522     Document Type: Article
Times cited : (24)

References (31)
  • 1
    • 0017338724 scopus 로고
    • Properties of carboxytransphosphorylase; pyruvate, phosphate dikinase; pyrophosphate-phosphofructikinase and pyrophosphate-acetate kinase and their roles in the metabolism of inorganic pyrophosphate
    • Wood, H. G., O'Brien, W. E., and Michaels, G. (1977) Properties of carboxytransphosphorylase; pyruvate, phosphate dikinase; pyrophosphate- phosphofructikinase and pyrophosphate-acetate kinase and their roles in the metabolism of inorganic pyrophosphate, Adv. Enzymol. 45, 85-155.
    • (1977) Adv. Enzymol. , vol.45 , pp. 85-155
    • Wood, H.G.1    O'Brien, W.E.2    Michaels, G.3
  • 2
    • 0025149777 scopus 로고
    • Determination of the catalytic pathway of C4-leaf pyruvate, orthophosphate dikinase from maize
    • Carroll, L. J., Dunaway-Mariano, D., Smith, C. M., and Chollet, R. (1990) Determination of the catalytic pathway of C4-leaf pyruvate, orthophosphate dikinase from maize, FEBS Lett. 274, 178-180.
    • (1990) FEBS Lett. , vol.274 , pp. 178-180
    • Carroll, L.J.1    Dunaway-Mariano, D.2    Smith, C.M.3    Chollet, R.4
  • 3
    • 0001258742 scopus 로고
    • The mode of triple phosphoryl group transfer in pyruvate phosphate dikinase catalysis. Demonstration of the intermediacy of pyrophosphorylated and phosphorylated enzyme species
    • Carroll, L. J., Mehl, A. F., and Dunaway-Mariano, D. (1989) The mode of triple phosphoryl group transfer in pyruvate phosphate dikinase catalysis. Demonstration of the intermediacy of pyrophosphorylated and phosphorylated enzyme species, J. Am. Chem. Soc. 111, 5965-5967.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 5965-5967
    • Carroll, L.J.1    Mehl, A.F.2    Dunaway-Mariano, D.3
  • 4
    • 0025606663 scopus 로고
    • Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs
    • Pocalyko, D. J., Carroll, L. J., Martin, B. M., Babbitt, P. C., and Dunaway-Mariano, D. (1990) Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs, Biochemistry 29, 10757-10765.
    • (1990) Biochemistry , vol.29 , pp. 10757-10765
    • Pocalyko, D.J.1    Carroll, L.J.2    Martin, B.M.3    Babbitt, P.C.4    Dunaway-Mariano, D.5
  • 5
    • 0024288485 scopus 로고
    • Primary structure of maize pyruvate, orthophosphate dikinase as deduced from cDNA sequence
    • Matsuoka, M., Ozeki, Y., Yamamoto, N., Hirano, H., Kano-Murakami, Y., and Tanaka, Y. (1988) Primary structure of maize pyruvate, orthophosphate dikinase as deduced from cDNA sequence, J. Biol. Chem. 263, 11080-11083.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11080-11083
    • Matsuoka, M.1    Ozeki, Y.2    Yamamoto, N.3    Hirano, H.4    Kano-Murakami, Y.5    Tanaka, Y.6
  • 6
    • 0029900511 scopus 로고    scopus 로고
    • Determination of the nucleotide binding site within Clostridlum symbiosum pyruvate phosphate dikinase by photoaffinity labeling, site-directed mutagenesis, and structural analysis
    • McGuire, M., Carroll, L. J., Yankie, L., Thrall, S. H., Dunaway-Mariano, D., Herzberg, O., Jayaram, B., and Haley, B. H. (1996) Determination of the nucleotide binding site within Clostridlum symbiosum pyruvate phosphate dikinase by photoaffinity labeling, site-directed mutagenesis, and structural analysis, Biochemistry 35, 8544-8552.
    • (1996) Biochemistry , vol.35 , pp. 8544-8552
    • McGuire, M.1    Carroll, L.J.2    Yankie, L.3    Thrall, S.H.4    Dunaway-Mariano, D.5    Herzberg, O.6    Jayaram, B.7    Haley, B.H.8
  • 7
    • 0032578501 scopus 로고    scopus 로고
    • Location of the phosphate binding site within Clostridium symbiosum pyruvate phosphate dikinase
    • McGuire, M., Huang, K., Kapadia, G., Herzberg, O., and Dunaway-Mariano, D. (1998) Location of the phosphate binding site within Clostridium symbiosum pyruvate phosphate dikinase, Biochemistry 37, 13463-13474.
    • (1998) Biochemistry , vol.37 , pp. 13463-13474
    • McGuire, M.1    Huang, K.2    Kapadia, G.3    Herzberg, O.4    Dunaway-Mariano, D.5
  • 8
    • 0028959020 scopus 로고
    • Separate site catalysis by pyruvate phosphate dikinase as revealed by deletion mutants
    • Xu, Y., McGuire, M., Dunaway-Mariano, D., and Martin, B. M. (1995) Separate site catalysis by pyruvate phosphate dikinase as revealed by deletion mutants, Biochemistry 34, 2195-2202.
    • (1995) Biochemistry , vol.34 , pp. 2195-2202
    • Xu, Y.1    McGuire, M.2    Dunaway-Mariano, D.3    Martin, B.M.4
  • 9
    • 0028957135 scopus 로고
    • Location of the catalytic site for phosphoenolpyruvate formation within the primary structure of Clostridium symbiosum pyruvate phosphate dikinase. 2. Site-directed mutagenesis of an essential arginine contained within an apparent P-loop
    • Yankie, L., Xu, Y., and Dunaway-Mariano, D. (1995) Location of the catalytic site for phosphoenolpyruvate formation within the primary structure of Clostridium symbiosum pyruvate phosphate dikinase. 2. Site-directed mutagenesis of an essential arginine contained within an apparent P-loop, Biochemistry 34, 2188-2194.
    • (1995) Biochemistry , vol.34 , pp. 2188-2194
    • Yankie, L.1    Xu, Y.2    Dunaway-Mariano, D.3
  • 11
    • 0035983518 scopus 로고    scopus 로고
    • The 3.0 Å resolution crystal structure of glycosomal pyruvate phosphate dikinase from Trypanosoma brucei
    • Cosenza, L. W., Bringaud, F., Baltz, T., and Vellieux, F. M. (2002) The 3.0 Å resolution crystal structure of glycosomal pyruvate phosphate dikinase from Trypanosoma brucei, J. Mol. Biol. 318, 1417-1432.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1417-1432
    • Cosenza, L.W.1    Bringaud, F.2    Baltz, T.3    Vellieux, F.M.4
  • 12
    • 0029950031 scopus 로고    scopus 로고
    • Structural classification of proteins: New superfamilies
    • Murzin, A. G. (1996) Structural classification of proteins: New superfamilies, Curr. Opin. Struct. Biol. 6, 386-394.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 386-394
    • Murzin, A.G.1
  • 13
    • 0027530140 scopus 로고
    • Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 Å resolution
    • Yamaguchi, H., Kato, H., Hata, Y., Nishioka, T., Kimura, A., Oda, J., and Katsube, Y. (1993) Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 Å resolution, J. Mol. Biol. 229, 1083-1100.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1083-1100
    • Yamaguchi, H.1    Kato, H.2    Hata, Y.3    Nishioka, T.4    Kimura, A.5    Oda, J.6    Katsube, Y.7
  • 14
    • 0036384350 scopus 로고    scopus 로고
    • One fold with many functions: The evolutionary relationships between TIM barrel families based on their sequences, structures and functions
    • Nagano, N., Orengo, C. A., and Thornton, J. M. (2002) One fold with many functions: The evolutionary relationships between TIM barrel families based on their sequences, structures and functions, J. Mol. Biol. 321, 741-765.
    • (2002) J. Mol. Biol. , vol.321 , pp. 741-765
    • Nagano, N.1    Orengo, C.A.2    Thornton, J.M.3
  • 15
    • 0037154102 scopus 로고    scopus 로고
    • Pyruvate site of pyruvate phosphate dikinase: Crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis
    • Herzberg, O., Chen, C. C., Liu, S., Tempczyk, A., Howard, A., Wei, M., Ye, D., and Dunaway-Mariano, D. (2002) Pyruvate site of pyruvate phosphate dikinase: Crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis, Biochemistry 41, 780-787.
    • (2002) Biochemistry , vol.41 , pp. 780-787
    • Herzberg, O.1    Chen, C.C.2    Liu, S.3    Tempczyk, A.4    Howard, A.5    Wei, M.6    Ye, D.7    Dunaway-Mariano, D.8
  • 16
    • 4344704970 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray diffraction studies on pyruvate phosphate dikinase from maize
    • Nakanishi, T., Ohki, Y., Oda, J., Matsuoka, M., Sakata, K., and Kato, H. (2004) Purification, crystallization and preliminary X-ray diffraction studies on pyruvate phosphate dikinase from maize, Acta Crystallogr. D60, 193-194.
    • (2004) Acta Crystallogr. D , vol.60 , pp. 193-194
    • Nakanishi, T.1    Ohki, Y.2    Oda, J.3    Matsuoka, M.4    Sakata, K.5    Kato, H.6
  • 17
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath, J. W. (1999) The finer things in X-ray diffraction data collection, Acta Crystallogr. D55, 1718-1725.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 20
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger, A. T. (1992) Free R value: A novel statistical quantity for assessing the accuracy of crystal structures, Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 21
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • 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.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 22
    • 0032215320 scopus 로고    scopus 로고
    • Databases in protein crystallography
    • Kleywegt, G. J., and Jones, T. A. (1998) Databases in protein crystallography, Acta Crystallogr. D54, 1119-1131.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 1119-1131
    • Kleywegt, G.J.1    Jones, T.A.2
  • 23
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme
    • Hayward, S., and Berendsen, H. J. (1998) Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme, Proteins 30, 144-154.
    • (1998) Proteins , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.2
  • 24
    • 0028276977 scopus 로고
    • The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-Å resolution
    • Wolodko, W. T., Fraser, M. E., James, M. N., and Bridger, W. A. (1994) The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-Å resolution, J. Biol. Chem. 269, 10883-10890.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10883-10890
    • Wolodko, W.T.1    Fraser, M.E.2    James, M.N.3    Bridger, W.A.4
  • 25
    • 0035813214 scopus 로고    scopus 로고
    • Investigation of the catalytic site within the ATP-grasp domain of Clostridium symbiosum pyruvate phosphate dikinase
    • Ye, D., Wei, M., McGuire, M., Huang, K., Kapadia, G., Herzberg, O., Martin, B. M., and Dunaway-Mariano, D. (2001) Investigation of the catalytic site within the ATP-grasp domain of Clostridium symbiosum pyruvate phosphate dikinase, J. Biol. Chem. 276, 37630-37639.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37630-37639
    • Ye, D.1    Wei, M.2    McGuire, M.3    Huang, K.4    Kapadia, G.5    Herzberg, O.6    Martin, B.M.7    Dunaway-Mariano, D.8
  • 27
    • 0035856542 scopus 로고    scopus 로고
    • Investigation of the role of the domain linkers in separate site catalysis by Clostridium symbiosum pyruvate phosphate dikinase
    • Wei, M., Ye, D., and Dunaway-Mariano, D. (2001) Investigation of the role of the domain linkers in separate site catalysis by Clostridium symbiosum pyruvate phosphate dikinase, Biochemistry 40, 13466-13473.
    • (2001) Biochemistry , vol.40 , pp. 13466-13473
    • Wei, M.1    Ye, D.2    Dunaway-Mariano, D.3
  • 29
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 30
    • 0000097225 scopus 로고    scopus 로고
    • SPOCK: Real-time collaborative molecular modelling
    • Christopher, B. T. (1998) SPOCK: Real-time collaborative molecular modelling, J. Mol. Graphics Modell. 16, 285-285.
    • (1998) J. Mol. Graphics Modell. , vol.16 , pp. 285-285
    • Christopher, B.T.1
  • 31
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A., and Bacon, D. J. (1997) Raster3D: Photorealistic Molecular Graphics, Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


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