메뉴 건너뛰기




Volumn 18, Issue 23, 1999, Pages 6809-6815

Redox signalling in the chloroplast: Structure of oxidized pea fructose-1,6-bisphosphate phosphatase

Author keywords

Allostery; Chloroplast; Photosynthesis; Redox regulation; Thioredoxin

Indexed keywords

DISULFIDE; FRUCTOSE 1,6 BISPHOSPHATE; PHOSPHATASE;

EID: 0033485824     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.23.6809     Document Type: Article
Times cited : (112)

References (46)
  • 2
    • 0002208132 scopus 로고
    • Crystallographic refinement by simulated annealing: Application to crambin
    • Brünger, A.T., Karplus, M. and Petsko, G.A. (1989) Crystallographic refinement by simulated annealing: application to crambin. Acta Crystallogr. A, 45, 50-61.
    • (1989) Acta Crystallogr. A , vol.45 , pp. 50-61
    • Brünger, A.T.1    Karplus, M.2    Petsko, G.A.3
  • 3
    • 0000765807 scopus 로고
    • Role of light in the regulation of chloroplast enzymes
    • Buchanan, B.B. (1980) Role of light in the regulation of chloroplast enzymes. Annu. Rev. Plant Physiol., 31, 341-374.
    • (1980) Annu. Rev. Plant Physiol. , vol.31 , pp. 341-374
    • Buchanan, B.B.1
  • 4
    • 0025923587 scopus 로고
    • 2 assimilation in oxygenic photosynthesis: The ferredoxin/thioredoxin system. Perspective on its discovery, present status and future development
    • 2 assimilation in oxygenic photosynthesis: the ferredoxin/thioredoxin system. Perspective on its discovery, present status and future development. Arch. Biochem. Biophys., 288, 1-9.
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 1-9
    • Buchanan, B.B.1
  • 5
    • 0017096742 scopus 로고
    • Photosynthetic regulatory protein found in animal and bacterial cells
    • Buchanan, B.B. and Wolosiuk, R.A. (1976) Photosynthetic regulatory protein found in animal and bacterial cells. Nature, 264, 669-670.
    • (1976) Nature , vol.264 , pp. 669-670
    • Buchanan, B.B.1    Wolosiuk, R.A.2
  • 6
    • 0033561407 scopus 로고    scopus 로고
    • Chloroplast NADP-malate dehydrogenase: Structural basis of light-dependent regulation of activity by thiol oxidation and reduction
    • Carr, P.D., Verger, D., Ashton, A.R. and Ollis, D.L. (1999) Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction. Structure, 7, 461-475.
    • (1999) Structure , vol.7 , pp. 461-475
    • Carr, P.D.1    Verger, D.2    Ashton, A.R.3    Ollis, D.L.4
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Program for protein crystallography
    • (1994) The CCP4 suite: program for protein crystallography. Acta Crystallogr. D, 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 8
    • 0027131734 scopus 로고
    • Site-specific mutagenesis of the metal binding sites of porcine fructose-1,6-bisphosphatase
    • Chen, L., Hegde, R., Chen, M. and Fromm, H.J. (1993) Site-specific mutagenesis of the metal binding sites of porcine fructose-1,6-bisphosphatase. Arch. Biochem. Biophys., 307, 350-354.
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 350-354
    • Chen, L.1    Hegde, R.2    Chen, M.3    Fromm, H.J.4
  • 9
    • 0023411440 scopus 로고
    • The pAR5 mutation and the allosteric mechanism of Escherichia coli aspartate carbamoyltransferase
    • Cherfils, J., Vachette, P., Tauc, P. and Janin, J. (1987) The pAR5 mutation and the allosteric mechanism of Escherichia coli aspartate carbamoyltransferase. EMBO J., 6, 2843-2847.
    • (1987) EMBO J. , vol.6 , pp. 2843-2847
    • Cherfils, J.1    Vachette, P.2    Tauc, P.3    Janin, J.4
  • 10
    • 0032544209 scopus 로고    scopus 로고
    • Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase
    • Choe, J.Y., Poland, B.W., Fromm, H.J. and Honzatko, R.B. (1998) Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase. Biochemistry, 37, 11441-11450.
    • (1998) Biochemistry , vol.37 , pp. 11441-11450
    • Choe, J.Y.1    Poland, B.W.2    Fromm, H.J.3    Honzatko, R.B.4
  • 11
    • 0032430304 scopus 로고    scopus 로고
    • Location of the redox-active cysteines in chloroplast sedoheptulose-1,7-bisphophatase indicates that its allosteric regulation is similar but not identical to that of fructose-1,6-bisphosphatase
    • Dunford, R.P., Durrant, M.C., Catley, M.A. and Dyerj, A. (1998) Location of the redox-active cysteines in chloroplast sedoheptulose-1,7-bisphophatase indicates that its allosteric regulation is similar but not identical to that of fructose-1,6-bisphosphatase. Photosynth. Res., 58, 221-230.
    • (1998) Photosynth. Res. , vol.58 , pp. 221-230
    • Dunford, R.P.1    Durrant, M.C.2    Catley, M.A.3    Dyerj, A.4
  • 12
    • 0032538317 scopus 로고    scopus 로고
    • Structural basis for activation of ARF GTPase: Mechanisms of guanine nucleotide exchange and GTP-myristoyl switching
    • Goldberg, J. (1998) Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching. Cell, 95, 237-248.
    • (1998) Cell , vol.95 , pp. 237-248
    • Goldberg, J.1
  • 13
    • 0033600744 scopus 로고    scopus 로고
    • Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-κB
    • Hirota, K., Murata, M., Sachi, Y., Nakamura, H., Takeuchi, J., Mori, K. and Yodoi, J. (1999) Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-κB. J. Biol. Chem., 274, 27891-27897.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27891-27897
    • Hirota, K.1    Murata, M.2    Sachi, Y.3    Nakamura, H.4    Takeuchi, J.5    Mori, K.6    Yodoi, J.7
  • 14
    • 85047691615 scopus 로고
    • High-level expression of recombinant pea chloroplast fructose-1,6-bisphosphatase and mutagenesis of its regulatory site
    • Jacquot, J.P. et al. (1995) High-level expression of recombinant pea chloroplast fructose-1,6-bisphosphatase and mutagenesis of its regulatory site. Eur. J. Biochem., 229, 675-681.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 675-681
    • Jacquot, J.P.1
  • 15
    • 0031444519 scopus 로고    scopus 로고
    • Thioredoxins: Structure and function in plant cells
    • Jacquot, J.P., Lancelin, J.M. and Meyer, Y. (1997a) Thioredoxins: structure and function in plant cells. New Phytol., 136, 543-570.
    • (1997) New Phytol. , vol.136 , pp. 543-570
    • Jacquot, J.P.1    Lancelin, J.M.2    Meyer, Y.3
  • 17
    • 0033528714 scopus 로고    scopus 로고
    • Structural basis for light activation of a chloroplast enzyme: The structure of sorghum NADP-malate dehydrogenase in its oxidized form
    • Johansson, K., Ramaswamy, S., Saarinen, M., Lemaire-Chamley, M., Issakidis-Bourguet, E., Miginiac-Maslow, M. and Eklund, H. (1999) Structural basis for light activation of a chloroplast enzyme: the structure of sorghum NADP-malate dehydrogenase in its oxidized form. Biochemistry, 38, 4319-4326.
    • (1999) Biochemistry , vol.38 , pp. 4319-4326
    • Johansson, K.1    Ramaswamy, S.2    Saarinen, M.3    Lemaire-Chamley, M.4    Issakidis-Bourguet, E.5    Miginiac-Maslow, M.6    Eklund, H.7
  • 18
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A, 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 19
    • 0032889677 scopus 로고    scopus 로고
    • Redox regulation in cellular signalling
    • Kamata, H. and Hirata, H. (1999) Redox regulation in cellular signalling. Cell. Signal., 11, 1-14.
    • (1999) Cell. Signal. , vol.11 , pp. 1-14
    • Kamata, H.1    Hirata, H.2
  • 20
    • 0025160386 scopus 로고
    • Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP and magnesium
    • Ke, H.M., Zhang, Y.P. and Lipscomb, W.N. (1990) Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP and magnesium. Proc. Natl. Acad. Sci. USA, 87, 5243-5247.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5243-5247
    • Ke, H.M.1    Zhang, Y.P.2    Lipscomb, W.N.3
  • 21
    • 0025883747 scopus 로고
    • Conformational transition of fructose-1,6-bisphosphatase: Structure comparison between the AMP complex (T form) and the fructose 6-phosphate complex (R form)
    • Ke, H.M., Liang, J.Y., Zhang, Y.P. and Lipscomb, W.N. (1991a) Conformational transition of fructose-1,6-bisphosphatase: structure comparison between the AMP complex (T form) and the fructose 6-phosphate complex (R form). Biochemistry, 30, 4412-4420.
    • (1991) Biochemistry , vol.30 , pp. 4412-4420
    • Ke, H.M.1    Liang, J.Y.2    Zhang, Y.P.3    Lipscomb, W.N.4
  • 22
    • 0026347534 scopus 로고
    • Crystal structure of the neutral form of fructose-1,6-bisphosphatase complexed with the product fructose 6-phosphate at 2.1-Å resolution
    • Ke, H.M., Zhang, Y.P., Liang, J.Y. and Lipscomb, W.N. (1991b) Crystal structure of the neutral form of fructose-1,6-bisphosphatase complexed with the product fructose 6-phosphate at 2.1-Å resolution. Proc. Natl Acad. Sci. USA, 88, 2989-2993.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2989-2993
    • Ke, H.M.1    Zhang, Y.P.2    Liang, J.Y.3    Lipscomb, W.N.4
  • 24
    • 0002832337 scopus 로고
    • Structure and function of allosteric enzymes
    • Lipscomb, W.N. (1991) Structure and function of allosteric enzymes. Chemtracts Biochem. Mol. Biol., 2, 1-15.
    • (1991) Chemtracts Biochem. Mol. Biol. , vol.2 , pp. 1-15
    • Lipscomb, W.N.1
  • 25
    • 0024058280 scopus 로고
    • Comparative amino acid sequence of fructose-1,6-bisphosphatases: Identification of a region unique to the light-regulated chloroplast enzyme
    • Marcus, F., Moberly, L. and Latshaw, S.P. (1988) Comparative amino acid sequence of fructose-1,6-bisphosphatases: identification of a region unique to the light-regulated chloroplast enzyme. Proc. Natl Acad. Sci. USA, 85, 5379-5383.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 5379-5383
    • Marcus, F.1    Moberly, L.2    Latshaw, S.P.3
  • 27
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994) AMoRe: an automated package for molecular replacement. Acta Crystallogr. A, 50, 157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 28
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • Sawyer, L., Isaacs, N. and Bailey, S. (eds), Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1993) Oscillation data reduction program. In Sawyer, L., Isaacs, N. and Bailey, S. (eds), CCP4 Study Weekend: Data Collection and Processing. Daresbury Laboratory, Warrington, UK, pp. 56-62.
    • (1993) CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 29
    • 84980186051 scopus 로고
    • Light-dark transients in levels of intermediate compounds during photosynthesis in air adapted
    • Pedersen, T.A., Kirk, M. and Bassham, J. (1966) Light-dark transients in levels of intermediate compounds during photosynthesis in air adapted Chlorella. Physiol. Plant., 19, 219-231.
    • (1966) Chlorella. Physiol. Plant. , vol.19 , pp. 219-231
    • Pedersen, T.A.1    Kirk, M.2    Bassham, J.3
  • 30
    • 0019403247 scopus 로고
    • On the activation of fructose-1,6-bisphosphatase of spinach chloroplasts and the regulation of the Calvin cycle
    • Pradel, J., Soulie, J.M., Buc, J., Meunier, J.C. and Ricard, J. (1981) On the activation of fructose-1,6-bisphosphatase of spinach chloroplasts and the regulation of the Calvin cycle. Eur. J. Biochem., 113, 507-511.
    • (1981) Eur. J. Biochem. , vol.113 , pp. 507-511
    • Pradel, J.1    Soulie, J.M.2    Buc, J.3    Meunier, J.C.4    Ricard, J.5
  • 31
    • 0029644240 scopus 로고
    • Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF-κB
    • Qin, J., Clore, G.M., Kennedy, W.M., Huth, J.R. and Gronenborn, A.M. (1995) Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF-κB. Structure, 3, 289-297.
    • (1995) Structure , vol.3 , pp. 289-297
    • Qin, J.1    Clore, G.M.2    Kennedy, W.M.3    Huth, J.R.4    Gronenborn, A.M.5
  • 32
    • 0024297099 scopus 로고
    • Chloroplast fructose-1,6-bisphosphatase: The product of a mosaic gene
    • Raines, C.A., Lloyd, J.C., Longstaff, M., Bradley, D. and Dyer, T. (1988) Chloroplast fructose-1,6-bisphosphatase: the product of a mosaic gene. Nucleic Acids Res., 16, 7931-7942.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7931-7942
    • Raines, C.A.1    Lloyd, J.C.2    Longstaff, M.3    Bradley, D.4    Dyer, T.5
  • 33
    • 0031575848 scopus 로고    scopus 로고
    • Characterization of cysteine residues involved in the reductive activation and the structural stability of rapeseed (Brassica napus) chloroplast fructose-1,6-bisphosphatase
    • Rodriguez-Suarez, R.J., Mora-Garcia, S. and Wolosiuk, R.A. (1997) Characterization of cysteine residues involved in the reductive activation and the structural stability of rapeseed (Brassica napus) chloroplast fructose-1,6-bisphosphatase. Biochem. Biophys. Res. Commun., 232, 388-393.
    • (1997) Biochem. Biophys. Res. Commun. , vol.232 , pp. 388-393
    • Rodriguez-Suarez, R.J.1    Mora-Garcia, S.2    Wolosiuk, R.A.3
  • 34
    • 0032922625 scopus 로고    scopus 로고
    • Regulation of chloroplast enzyme activities by thioredoxins: Activation or relief from inhibition?
    • Ruelland, E. and Miginiac-Maslow, M. (1999) Regulation of chloroplast enzyme activities by thioredoxins: activation or relief from inhibition? Trends Plant Sci., 4, 136-141.
    • (1999) Trends Plant Sci. , vol.4 , pp. 136-141
    • Ruelland, E.1    Miginiac-Maslow, M.2
  • 36
    • 0017913406 scopus 로고
    • Studies on the regulatory properties of chloroplast fructose-1,6-bisphosphatase
    • Schurmann, P. and Wolosiuk, R.A. (1978) Studies on the regulatory properties of chloroplast fructose-1,6-bisphosphatase. Biochim. Biophys. Acta, 522, 130-138.
    • (1978) Biochim. Biophys. Acta , vol.522 , pp. 130-138
    • Schurmann, P.1    Wolosiuk, R.A.2
  • 37
    • 0029984062 scopus 로고    scopus 로고
    • Antioxidant and redox regulation of gene transcription
    • Sen, C.K. and Packer, L. (1996) Antioxidant and redox regulation of gene transcription. FASEB J., 10, 709-720.
    • (1996) FASEB J. , vol.10 , pp. 709-720
    • Sen, C.K.1    Packer, L.2
  • 38
    • 0025903710 scopus 로고
    • The mutation ß99 Asp-Tyr stabilizes Y-a new, composite quaternary state of human hemoglobin
    • Smith, F.R., Lattman, E.E. and Carter, C.W., Jr (1991) The mutation ß99 Asp-Tyr stabilizes Y-a new, composite quaternary state of human hemoglobin. Proteins, 10, 81-91.
    • (1991) Proteins , vol.10 , pp. 81-91
    • Smith, F.R.1    Lattman, E.E.2    Carter C.W., Jr.3
  • 39
    • 0017161211 scopus 로고
    • High resolution x-ray structure of yeast hexokinase, an allosteric protein exhibiting a non-symmetric arrangement of subunits
    • Steitz, T.A., Fletterick, R.J., Anderson, W.F. and Anderson, C.M. (1976) High resolution X-ray structure of yeast hexokinase, an allosteric protein exhibiting a non-symmetric arrangement of subunits. J. Mol. Biol., 104, 197-222.
    • (1976) J. Mol. Biol. , vol.104 , pp. 197-222
    • Steitz, T.A.1    Fletterick, R.J.2    Anderson, W.F.3    Anderson, C.M.4
  • 40
    • 0028922940 scopus 로고
    • Crystal structure of spinach chloroplast fructose-1,6-bisphosphatase at 2.8 Å resolution
    • Villeret, V., Huang, S., Zhang, Y., Xue, Y. and Lipscomb, W.N. (1995) Crystal structure of spinach chloroplast fructose-1,6-bisphosphatase at 2.8 Å resolution. Biochemistry, 34, 4299-4306.
    • (1995) Biochemistry , vol.34 , pp. 4299-4306
    • Villeret, V.1    Huang, S.2    Zhang, Y.3    Xue, Y.4    Lipscomb, W.N.5
  • 43
    • 0033529948 scopus 로고    scopus 로고
    • Mechanism of light regulation of rubisco: A specific role for the larger rubisco activase isoform involving reductive activation by thioredoxin-f
    • Zhang, N. and Portis, A.R., Jr (1999) Mechanism of light regulation of rubisco: a specific role for the larger rubisco activase isoform involving reductive activation by thioredoxin-f. Proc. Natl Acad. Sci. USA, 96, 9438-9443.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 9438-9443
    • Zhang, N.1    Portis A.R., Jr.2
  • 44
    • 0027458881 scopus 로고
    • Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase
    • Zhang, Y., Liang, J.Y., Huang, S., Ke, H. and Lipscomb, W.N. (1993) Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase. Biochemistry, 32, 1844-1857.
    • (1993) Biochemistry , vol.32 , pp. 1844-1857
    • Zhang, Y.1    Liang, J.Y.2    Huang, S.3    Ke, H.4    Lipscomb, W.N.5
  • 45
    • 0028029482 scopus 로고
    • Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphatase
    • Zhang, Y., Liang, J.Y., Huang, S. and Lipscomb, W.N. (1994) Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphatase. J. Mol. Biol., 244, 609-624.
    • (1994) J. Mol. Biol. , vol.244 , pp. 609-624
    • Zhang, Y.1    Liang, J.Y.2    Huang, S.3    Lipscomb, W.N.4
  • 46
    • 0017308249 scopus 로고
    • Efficient purification and molecular properties of spinach chloroplast fructose-1,6-bisphosphatase
    • Zimmermann, G., Kelly, G.J. and Latzko, E. (1976) Efficient purification and molecular properties of spinach chloroplast fructose-1,6-bisphosphatase. Eur. J. Biochem., 70, 361-367.
    • (1976) Eur. J. Biochem. , vol.70 , pp. 361-367
    • Zimmermann, G.1    Kelly, G.J.2    Latzko, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.