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Volumn 44, Issue 1, 2005, Pages 113-120

Altered intersubunit interactions in crystal structures of catalytically compromised ribulose-1,5-bisphosphate carboxylase/oxygenase

Author keywords

[No Author keywords available]

Indexed keywords

ALGAE; CARBOXYLATION; CATALYSTS; CRYSTAL STRUCTURE; PHOTOSYNTHESIS; STRUCTURAL ANALYSIS; THERMODYNAMIC STABILITY;

EID: 11844307195     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047928e     Document Type: Article
Times cited : (18)

References (42)
  • 1
    • 0037001967 scopus 로고    scopus 로고
    • Rubisco: Structure, regulatory interactions, and possibilities for a better enzyme
    • Spreitzer, R. J., and Salvucci, M. E. (2002) Rubisco: Structure, regulatory interactions, and possibilities for a better enzyme, Annu. Rev. Plant Biol. 53, 449-475.
    • (2002) Annu. Rev. Plant Biol. , vol.53 , pp. 449-475
    • Spreitzer, R.J.1    Salvucci, M.E.2
  • 3
    • 0037561915 scopus 로고    scopus 로고
    • Structural framework for catalysis and regulation in ribulose-1,5- bisphosphate carboxylase/oxygenase
    • Andersson, I., and Taylor, T. C. (2003) Structural framework for catalysis and regulation in ribulose-1,5-bisphosphate carboxylase/oxygenase, Arch. Biochem. Biophys. 414, 130-140.
    • (2003) Arch. Biochem. Biophys. , vol.414 , pp. 130-140
    • Andersson, I.1    Taylor, T.C.2
  • 4
    • 0038576219 scopus 로고    scopus 로고
    • Manipulating ribulose bisphosphate carboxylase/oxygenase in the chloroplasts of higher plants
    • Andrews, T. J., and Whitney, S. M. (2003) Manipulating ribulose bisphosphate carboxylase/oxygenase in the chloroplasts of higher plants. Arch. Biochem. Biophys. 414, 159-169.
    • (2003) Arch. Biochem. Biophys. , vol.414 , pp. 159-169
    • Andrews, T.J.1    Whitney, S.M.2
  • 6
    • 0032817398 scopus 로고    scopus 로고
    • Questions about the complexity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Spreitzer, R. J. (1999) Questions about the complexity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase, Photosynth. Res. 60, 29-42.
    • (1999) Photosynth. Res. , vol.60 , pp. 29-42
    • Spreitzer, R.J.1
  • 7
    • 0019470148 scopus 로고
    • Species variation in the specificity of ribulose biphosphate carboxylase/oxygenase
    • Jordan, D. B., and Ogren, W. L. (1981) Species variation in the specificity of ribulose biphosphate carboxylase/oxygenase, Nature 297, 513-515.
    • (1981) Nature , vol.297 , pp. 513-515
    • Jordan, D.B.1    Ogren, W.L.2
  • 8
    • 0028085941 scopus 로고
    • High substrate-specificity factor ribulose-bisphosphate carboxylase oxygenase from eukaryotic marine-algae and properties of recombinant cyanobacterial rubisco containing algal residue modifications
    • Read, B. A., and Tabita, F. R. (1994) High substrate-specificity factor ribulose-bisphosphate carboxylase oxygenase from eukaryotic marine-algae and properties of recombinant cyanobacterial rubisco containing algal residue modifications, Arch. Biochem. Biophys. 312, 210-218.
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 210-218
    • Read, B.A.1    Tabita, F.R.2
  • 11
    • 0038237435 scopus 로고    scopus 로고
    • Role of the Rubisco small subunit
    • Spreitzer, R. J. (2003) Role of the Rubisco small subunit, Arch. Biochem. Biophys. 414, 141-149.
    • (2003) Arch. Biochem. Biophys. , vol.414 , pp. 141-149
    • Spreitzer, R.J.1
  • 12
    • 0002104076 scopus 로고    scopus 로고
    • Leegood, R. C., Sharkey, T. D., and von Caemmerer, S., Eds. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Roy, H., and Andrews, T. J. (2000) in Photosynthesis: Physiology and metabolism (Leegood, R. C., Sharkey, T. D., and von Caemmerer, S., Eds.) pp 53-83, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (2000) Photosynthesis: Physiology and Metabolism , pp. 53-83
    • Roy, H.1    Andrews, T.J.2
  • 13
    • 0032818243 scopus 로고    scopus 로고
    • Plastome engineering of ribulose-1,5-bisphosphate carboxylase/oxygenase in tobacco to form a sunflower large subunit and tobacco small subunit hybrid
    • Kanevski, I., Maliga, P., Rhoades, D. F., and Gutteridge, S. (1999) Plastome engineering of ribulose-1,5-bisphosphate carboxylase/oxygenase in tobacco to form a sunflower large subunit and tobacco small subunit hybrid, Plant Physiol. 119, 133-141.
    • (1999) Plant Physiol. , vol.119 , pp. 133-141
    • Kanevski, I.1    Maliga, P.2    Rhoades, D.F.3    Gutteridge, S.4
  • 14
    • 0033212939 scopus 로고    scopus 로고
    • Directed mutation of the Rubisco large subunit of tobacco influences photorespiration and growth
    • Whitney, S. M., von Caemmerer, S., Hudson, G. S., and Andrews, T. J. (1999) Directed mutation of the Rubisco large subunit of tobacco influences photorespiration and growth, Plant Physiol. 121, 579-588.
    • (1999) Plant Physiol. , vol.121 , pp. 579-588
    • Whitney, S.M.1    Von Caemmerer, S.2    Hudson, G.S.3    Andrews, T.J.4
  • 15
    • 0028245595 scopus 로고
    • Structure, function, regulation, and assembly of D-ribulose-1,5- bisphosphate carboxylase oxygenase
    • Hartman, F. C., and Harpel, M. R. (1994) Structure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase oxygenase, Annu. Rev. Biochem. 63, 197-234.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 197-234
    • Hartman, F.C.1    Harpel, M.R.2
  • 17
    • 0000170741 scopus 로고
    • Thermal-instability of ribulose-1,5-bisphosphate carboxylase oxygenase from a temperature-conditional chloroplast mutant of Chlamydomonas reinhardtii
    • Chen, Z., Hong, S., and Spreitzer, R. J. (1993) Thermal-instability of ribulose-1,5-bisphosphate carboxylase oxygenase from a temperature-conditional chloroplast mutant of Chlamydomonas reinhardtii, Plant Physiol. 101, 1189-1194.
    • (1993) Plant Physiol. , vol.101 , pp. 1189-1194
    • Chen, Z.1    Hong, S.2    Spreitzer, R.J.3
  • 18
    • 0030967199 scopus 로고    scopus 로고
    • Complementing substitutions at the bottom of the barrel influence catalysis and stability of ribulose-bisphosphate carboxylase/oxygenase
    • Hong, S., and Spreitzer, R. J. (1997) Complementing substitutions at the bottom of the barrel influence catalysis and stability of ribulose-bisphosphate carboxylase/oxygenase, J. Biol. Chem. 272, 11114-11117.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11114-11117
    • Hong, S.1    Spreitzer, R.J.2
  • 19
    • 0034733507 scopus 로고    scopus 로고
    • Suppressor mutations in the chloroplast-encoded large subunit improve the thermal stability of wild-type ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Du, Y. C., and Spreitzer, R. J. (2000) Suppressor mutations in the chloroplast-encoded large subunit improve the thermal stability of wild-type ribulose-1,5-bisphosphate carboxylase/oxygenase, J. Biol. Chem. 275, 19844-19847.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19844-19847
    • Du, Y.C.1    Spreitzer, R.J.2
  • 20
    • 0000709041 scopus 로고
    • Photosynthesis-deficient mutants of Chlamydomonas reinhardtii with associated light-sensitive phenotypes
    • Spreitzer, R. J., and Mets, L. (1981) Photosynthesis-deficient mutants of Chlamydomonas reinhardtii with associated light-sensitive phenotypes, Plant Physiol. 67, 565-569.
    • (1981) Plant Physiol. , vol.67 , pp. 565-569
    • Spreitzer, R.J.1    Mets, L.2
  • 21
    • 0035930525 scopus 로고    scopus 로고
    • First crystal structure of Rubisco from a green alga - Chlamydomonas reinhardtii
    • Taylor, T. C., Backlund, A., Björhall, K., Spreitzer, R. J., and Andersson, I. (2001) First crystal structure of Rubisco from a green alga - Chlamydomonas reinhardtii, J. Biol. Chem. 276, 48159-48164.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48159-48164
    • Taylor, T.C.1    Backlund, A.2    Björhall, K.3    Spreitzer, R.J.4    Andersson, I.5
  • 22
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 23
    • 0031053055 scopus 로고    scopus 로고
    • AMoRe: An automated molecular replacement program package
    • Navaza, J., and Saludjian, P. (1997) AMoRe: An automated molecular replacement program package, Methods Enzymol. 276, 581-594.
    • (1997) Methods Enzymol. , vol.276 , pp. 581-594
    • Navaza, J.1    Saludjian, P.2
  • 24
    • 0028103275 scopus 로고
    • The CCP4 suite-programs for protein crystallography
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite-programs for protein crystallography, Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 25
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D53, 240-255.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 26
    • 0030809260 scopus 로고    scopus 로고
    • wARP: Improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models
    • Perrakis, A., Sixma, T. K., Wilson, K. S., and Lamzin, V. S. (1997) wARP: Improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models, Acta Crystallogr. D53, 448, 659-455.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 448
    • Perrakis, A.1    Sixma, T.K.2    Wilson, K.S.3    Lamzin, V.S.4
  • 27
    • 0000649842 scopus 로고    scopus 로고
    • Improved structure refinement through maximum likelihood
    • Pannu, N. S., and Read, R. J. (1996) Improved structure refinement through maximum likelihood, Acta Crystallogr. A52, 659-668.
    • (1996) Acta Crystallogr. , vol.A52 , pp. 659-668
    • Pannu, N.S.1    Read, R.J.2
  • 28
    • 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. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecules
    • Kleywegt, G. J., and Jones, T. A. (1994) Detection, delineation, measurement and display of cavities in macromolecules, Acta Crystallogr. D50, 178-185.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 30
    • 0034903751 scopus 로고    scopus 로고
    • Molray - A web interface between O and POV-Ray ray tracer
    • Harris, M., and Jones, T. A. (2001) Molray - a web interface between O and POV-Ray ray tracer, Acta Crystallogr. D57, 1201-1203.
    • (2001) Acta Crystallogr. , vol.D57 , pp. 1201-1203
    • Harris, M.1    Jones, T.A.2
  • 31
    • 0031592468 scopus 로고    scopus 로고
    • The structure of the complex between rubisco and its natural substrate ribulose-1,5-bisphosphate
    • Taylor, T. C., and Andersson, I. (1997) The structure of the complex between rubisco and its natural substrate ribulose-1,5-bisphosphate, J. Mol. Biol. 265, 432-444.
    • (1997) J. Mol. Biol. , vol.265 , pp. 432-444
    • Taylor, T.C.1    Andersson, I.2
  • 32
    • 0036304148 scopus 로고    scopus 로고
    • Crystal structure of activated ribulose-1,5-bisphosphate carboxylase/oxygenase from green alga Chlamydomonas reinhardtii complexed with 2-carboxyarabinitol-1,5-bisphosphate
    • Mizohata, E., Matsumura, H., Okano, Y., Kumei, M., Takuma, H., Onodera, J., Kato, K., Shibata, N., Inoue, T., Yokota, A., and Kai, Y. (2002) Crystal structure of activated ribulose-1,5-bisphosphate carboxylase/oxygenase from green alga Chlamydomonas reinhardtii complexed with 2-carboxyarabinitol-1,5- bisphosphate, J. Mol. Biol. 316, 679-691.
    • (2002) J. Mol. Biol. , vol.316 , pp. 679-691
    • Mizohata, E.1    Matsumura, H.2    Okano, Y.3    Kumei, M.4    Takuma, H.5    Onodera, J.6    Kato, K.7    Shibata, N.8    Inoue, T.9    Yokota, A.10    Kai, Y.11
  • 34
    • 1542677027 scopus 로고    scopus 로고
    • Assessment of structural and functional divergence far from the large-subunit active site of ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Du, Y. C., Peddi, S. R., and Spreitzer, R. J. (2003) Assessment of structural and functional divergence far from the large-subunit active site of ribulose-1,5-bisphosphate carboxylase/oxygenase, J. Biol. Chem. 278, 49401-49405.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49401-49405
    • Du, Y.C.1    Peddi, S.R.2    Spreitzer, R.J.3
  • 35
    • 0034687777 scopus 로고    scopus 로고
    • 2 specificity of rbcL-mutant ribulose-1,5-bisphosphate carboxylase/oxygenase
    • 2 specificity of rbcL-mutant ribulose-1,5-bisphosphate carboxylase/oxygenase, Proc. Natl. Acad. Sci. U.S.A. 97, 14206-14211.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 14206-14211
    • Du, Y.C.1    Hong, S.2    Spreitzer, R.J.3
  • 38
    • 0025160560 scopus 로고
    • Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4 Å resolution: Subunit interactions and the active site
    • Knight, S., Andersson, I., and Brändén, C.-I. (1990) Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4 Å resolution: subunit interactions and the active site. J. Mol. Biol. 215, 113-160.
    • (1990) J. Mol. Biol. , vol.215 , pp. 113-160
    • Knight, S.1    Andersson, I.2    Brändén, C.-I.3
  • 39
    • 0019316283 scopus 로고
    • Interaction of ribulosebisphosphate carboxylase/oxygenase with transition-state analogues
    • Pierce, J., Tolbert, N. E., and Barker, R. (1980) Interaction of ribulosebisphosphate carboxylase/oxygenase with transition-state analogues, Biochemistry 19, 934-942.
    • (1980) Biochemistry , vol.19 , pp. 934-942
    • Pierce, J.1    Tolbert, N.E.2    Barker, R.3
  • 41
    • 0033006446 scopus 로고    scopus 로고
    • The crystal structure of Rubisco from Alcaligenes eutrophus reveals a novel central eight-stranded β-barrel formed by β-strands from four subunits
    • Hansen, S., Burkow Vollan, V., Hough, E., and Andersen, K. (1999) The crystal structure of Rubisco from Alcaligenes eutrophus reveals a novel central eight-stranded β-barrel formed by β-strands from four subunits, J. Mol. Biol. 288, 609-621.
    • (1999) J. Mol. Biol. , vol.288 , pp. 609-621
    • Hansen, S.1    Burkow Vollan, V.2    Hough, E.3    Andersen, K.4
  • 42
    • 0033056852 scopus 로고    scopus 로고
    • Crystal structure of carboxylase reaction-oriented ribulose-1,5- bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria partita
    • Sugawara, H., Yamamoto, H., Shibata, N., Inoue, T., Okada, S., Miyake, C., Yokota, A., and Kai, Y. (1999) Crystal structure of carboxylase reaction-oriented ribulose-1,5-bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria partita, J. Biol. Chem. 274, 15655-15661.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15655-15661
    • Sugawara, H.1    Yamamoto, H.2    Shibata, N.3    Inoue, T.4    Okada, S.5    Miyake, C.6    Yokota, A.7    Kai, Y.8


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