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Volumn 44, Issue 29, 2005, Pages 9851-9861

Chimeric small subunits influence catalysis without causing global conformational changes in the crystal structure of ribulose-1,5-bisphosphate carboxylase/oxygenase

Author keywords

[No Author keywords available]

Indexed keywords

ALGAE; CARBOXYLATION; CATALYSIS; CRYSTAL STRUCTURE; PHOTOSYNTHESIS; PLANTS (BOTANY); X RAY CRYSTALLOGRAPHY;

EID: 22744434749     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050537v     Document Type: Article
Times cited : (44)

References (57)
  • 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
  • 2
    • 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
  • 3
    • 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
  • 5
    • 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
  • 7
    • 0019470148 scopus 로고
    • Species variation in the specificity of ribulosebisphosphate carboxylase/oxygenase
    • Jordan, D. B., and Ogren, W. L. (1981) Species variation in the specificity of ribulosebisphosphate carboxylase/oxygenase, Nature 297, 513-515.
    • (1981) Nature , vol.297 , pp. 513-515
    • Jordan, D.B.1    Ogren, W.L.2
  • 8
    • 0026643280 scopus 로고
    • A hybrid ribulosebisphosphate carboxylase/oxygenase enzyme exhibiting a substantial increase in substrate specificity factor
    • Read, B. A., and Tabita, F. R. (1992) A hybrid ribulosebisphosphate carboxylase/oxygenase enzyme exhibiting a substantial increase in substrate specificity factor, Biochemistry 31, 5553-5559.
    • (1992) Biochemistry , vol.31 , pp. 5553-5559
    • Read, B.A.1    Tabita, F.R.2
  • 9
    • 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
  • 13
    • 3242740327 scopus 로고    scopus 로고
    • Single-cell C4 photosynthesis versus the dual-cell (Kranz) paradigm
    • Edwards, G. E., Franceschi, V. R., and Voznesenskaya, E. V. (2004) Single-cell C4 photosynthesis versus the dual-cell (Kranz) paradigm, Annu. Rev. Plant Biol. 55, 173-196.
    • (2004) Annu. Rev. Plant Biol. , vol.55 , pp. 173-196
    • Edwards, G.E.1    Franceschi, V.R.2    Voznesenskaya, E.V.3
  • 14
    • 0035930525 scopus 로고    scopus 로고
    • First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii
    • Taylor, T. C., Backlund, A., Bjorhall, K., Spreitzer, R. J., and Anderson, 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    Bjorhall, K.3    Spreitzer, R.J.4    Anderson, I.5
  • 15
    • 0030003964 scopus 로고    scopus 로고
    • Large structures at high resolution: The 1.6 Å crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate
    • Andersson, I. (1996) Large structures at high resolution: The 1.6 Å crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate, J. Mol. Biol. 259, 160-174.
    • (1996) J. Mol. Biol. , vol.259 , pp. 160-174
    • Andersson, I.1
  • 16
    • 0027433039 scopus 로고
    • The X-ray structure of Synechococcus ribulose-bisphosphate carboxylase/oxygenase-activated quaternary complex at 2.2-Å resolution
    • Newman, J., and Gutteridge, S. (1993) The X-ray structure of Synechococcus ribulose-bisphosphate carboxylase/oxygenase-activated quaternary complex at 2.2-Å resolution, J. Biol. Chem. 268, 25876-25886.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25876-25886
    • Newman, J.1    Gutteridge, S.2
  • 17
    • 0027271860 scopus 로고
    • Crystal structure of activated tobacco rubisco complexed with the reaction-intermediate analogue 2-carboxyarabinitol 1,5-bisphosphate
    • Schreuder, H. A., Knight, S., Curmi, P. M. G., Andersson, I., Cascio, D., Sweet, R. M., Branden, C. I., and Eisenberg, D. (1993) Crystal structure of activated tobacco rubisco complexed with the reaction-intermediate analogue 2-carboxyarabinitol 1,5-bisphosphate, Protein Sci. 2, 1136-1146.
    • (1993) Protein Sci. , vol.2 , pp. 1136-1146
    • Schreuder, H.A.1    Knight, S.2    Curmi, P.M.G.3    Andersson, I.4    Cascio, D.5    Sweet, R.M.6    Branden, C.I.7    Eisenberg, D.8
  • 18
    • 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., Vollan, V. B., 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    Vollan, V.B.2    Hough, E.3    Andersen, K.4
  • 19
    • 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
  • 20
    • 0024617884 scopus 로고
    • Identification of an assembly domain in the small subunit of ribulose-1,5-bisphosphate carboxylase
    • Wasmann, C. C., Ramage, R. T., Bohnert, H. J., and Ostrem, J. A. (1989) Identification of an assembly domain in the small subunit of ribulose-1,5-bisphosphate carboxylase, Proc. Natl. Acad. Sci. U.S.A. 86, 1198-1202.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 1198-1202
    • Wasmann, C.C.1    Ramage, R.T.2    Bohnert, H.J.3    Ostrem, J.A.4
  • 21
    • 0026697599 scopus 로고
    • Replacement of a conserved arginine in the assembly domain of ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit interferes with holoenzyme formation
    • Flachmann, R., and Bohnert, H. J. (1992) Replacement of a conserved arginine in the assembly domain of ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit interferes with holoenzyme formation, J. Biol. Chem. 267, 10576-10582.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10576-10582
    • Flachmann, R.1    Bohnert, H.J.2
  • 22
    • 0029155277 scopus 로고
    • A mutation in the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase that reduces the rate of its incorporation into holoenzyme
    • Adam, Z. (1995) A mutation in the small subunit of ribulose-1,5- bisphosphate carboxylase/oxygenase that reduces the rate of its incorporation into holoenzyme, Photosynth. Res. 43, 143-147.
    • (1995) Photosynth. Res. , vol.43 , pp. 143-147
    • Adam, Z.1
  • 23
    • 0027744759 scopus 로고
    • Co-expression of plastid chaperonin genes and a synthetic plant Rubisco operon in Escherichia coli
    • Cloney, L. P., Bekkaoui, D. R., and Hemmingsen, S. M. (1993) Co-expression of plastid chaperonin genes and a synthetic plant Rubisco operon in Escherichia coli, Plant Mol. Biol. 23, 1285-1290.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 1285-1290
    • Cloney, L.P.1    Bekkaoui, D.R.2    Hemmingsen, S.M.3
  • 24
    • 0031992162 scopus 로고    scopus 로고
    • Chimeric Arabidopsis thaliana ribulose-1,5-bisphosphate carboxylase/oxygenase containing a pea small subunit protein is compromised in carbamylation
    • Getzoff, T. P., Zhu, G., Bohnert, H. J., and Jensen, R. G. (1998) Chimeric Arabidopsis thaliana ribulose-1,5-bisphosphate carboxylase/oxygenase containing a pea small subunit protein is compromised in carbamylation, Plant Physiol. 116, 695-702.
    • (1998) Plant Physiol. , vol.116 , pp. 695-702
    • Getzoff, T.P.1    Zhu, G.2    Bohnert, H.J.3    Jensen, R.G.4
  • 25
    • 0035101397 scopus 로고    scopus 로고
    • The gene for the ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) small subunit relocated to the plastid genome of tobacco directs the synthesis of small subunits that assemble into Rubisco
    • Whitney, S., and Andrews, T. (2001) The gene for the ribulose-1,5- bisphosphate carboxylase/oxygenase (Rubisco) small subunit relocated to the plastid genome of tobacco directs the synthesis of small subunits that assemble into Rubisco, Plant Cell 13, 193-205.
    • (2001) Plant Cell , vol.13 , pp. 193-205
    • Whitney, S.1    Andrews, T.2
  • 26
    • 0036857531 scopus 로고    scopus 로고
    • Complementation of the nuclear antisense rbcS-induced photosynthesis deficiency by introducing an rbcS gene into the tobacco plastid genome
    • Zhang, X. H., Ewy, R. G., Widholm, J. M., and Portis, A. R. (2002) Complementation of the nuclear antisense rbcS-induced photosynthesis deficiency by introducing an rbcS gene into the tobacco plastid genome, Plant Cell Physiol. 43, 1302-1313.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1302-1313
    • Zhang, X.H.1    Ewy, R.G.2    Widholm, J.M.3    Portis, A.R.4
  • 27
    • 0024039934 scopus 로고
    • 2 specificity of ribulose-1,5- bisphosphate carboxylase/oxygenase in a temperature-sensitive chloroplast mutant of Chlamydomonas reinhardtii
    • 2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase in a temperature-sensitive chloroplast mutant of Chlamydomonas reinhardtii, Proc. Natl. Acad. Sci. U.S.A. 85, 4696-4699.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 4696-4699
    • Chen, Z.1    Chastain, C.J.2    Al-Abed, S.R.3    Chollet, R.4    Spreitzer, R.J.5
  • 28
    • 0034687777 scopus 로고    scopus 로고
    • 2 specificity and thermal stability of rbcL-mutant ribulose-1,5-bisphosphate carboxylase/ oxygenase
    • 2 specificity and thermal stability 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
  • 29
    • 0030447478 scopus 로고    scopus 로고
    • Elimination of the Chlamydomonas gene family that encodes the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Khrebtukova, I., and Spreitzer, R. J. (1996) Elimination of the Chlamydomonas gene family that encodes the small subunit of ribulose-1,5- bisphosphate carboxylase/oxygenase, Proc. Natl. Acad. Sci. U.S.A. 93, 13689-13693.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 13689-13693
    • Khrebtukova, I.1    Spreitzer, R.J.2
  • 31
    • 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
  • 32
    • 0021943518 scopus 로고
    • Improved M13 phage cloning and host strains: Nucleotide sequence of the M13 mp19 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J., and Messing, J. (1985) Improved M13 phage cloning and host strains: Nucleotide sequence of the M13 mp19 and pUC19 vectors, Gene 33, 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 33
    • 0031893765 scopus 로고    scopus 로고
    • High-efficiency transformation of Chlamydomonas reinhardtii by electroporation
    • Shimogawara, K., Fujiwara, S., Grossman, A., and Usuda, H. (1998) High-efficiency transformation of Chlamydomonas reinhardtii by electroporation, Genetics 148, 1821-1828.
    • (1998) Genetics , vol.148 , pp. 1821-1828
    • Shimogawara, K.1    Fujiwara, S.2    Grossman, A.3    Usuda, H.4
  • 34
    • 0025637832 scopus 로고
    • Transformation of chloroplast ribosomal RNA genes in Chlamydomonas: Molecular and genetic characterization of integration events
    • Newman, S. M., Boynton, J. E., Gillham, N. W., Randolph-Anderson, B. L., Johnson, A. M., and Harris, E. H. (1990) Transformation of chloroplast ribosomal RNA genes in Chlamydomonas: Molecular and genetic characterization of integration events, Genetics 126, 875-888.
    • (1990) Genetics , vol.126 , pp. 875-888
    • Newman, S.M.1    Boynton, J.E.2    Gillham, N.W.3    Randolph-Anderson, B.L.4    Johnson, A.M.5    Harris, E.H.6
  • 35
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 36
    • 0001545770 scopus 로고
    • Heteroplasmic suppression of an amber mutation in the Chlamydomonas chloroplast gene that encodes the large subunit of ribulosebisphosphate carboxylase/oxygenase
    • Spreitzer, R. J., and Chastain, C. J. (1987) Heteroplasmic suppression of an amber mutation in the Chlamydomonas chloroplast gene that encodes the large subunit of ribulosebisphosphate carboxylase/oxygenase, Curr. Genet. 11, 611-616.
    • (1987) Curr. Genet. , vol.11 , pp. 611-616
    • Spreitzer, R.J.1    Chastain, C.J.2
  • 37
    • 0000269022 scopus 로고
    • Electrophoretic analysis of chloroplast proteins
    • Chua, N. H. (1980) Electrophoretic analysis of chloroplast proteins, Methods Enzymol. 69, 434-446.
    • (1980) Methods Enzymol. , vol.69 , pp. 434-446
    • Chua, N.H.1
  • 38
    • 0028150182 scopus 로고
    • 2 specificity of chloroplast ribulosebisphosphate carboxylase/oxygenase
    • 2 specificity of chloroplast ribulosebisphosphate carboxylase/oxygenase, Planta 193, 313-319.
    • (1994) Planta , vol.193 , pp. 313-319
    • Gotor, C.1    Hong, S.2    Spreitzer, R.J.3
  • 39
    • 0023953674 scopus 로고
    • Structure and expression of spinach leaf cDNA encoding ribulosebisphosphate carboxylase/oxygenase activase
    • Werneke, J. M., Zielinski, R. E., and Ogren, W. L. (1988) Structure and expression of spinach leaf cDNA encoding ribulosebisphosphate carboxylase/oxygenase activase, Proc. Natl. Acad. Sci. U.S.A. 85, 787-791.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 787-791
    • Werneke, J.M.1    Zielinski, R.E.2    Ogren, W.L.3
  • 40
    • 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
  • 41
    • 0000240773 scopus 로고
    • A sensitive assay procedure for simultaneous determination of ribulose-1,5-bisphosphate carboxylase and oxygenase activity
    • Jordan, D. B., and Ogren, W. L. (1981) A sensitive assay procedure for simultaneous determination of ribulose-1,5-bisphosphate carboxylase and oxygenase activity, Plant Physiol. 67, 237-245.
    • (1981) Plant Physiol. , vol.67 , pp. 237-245
    • Jordan, D.B.1    Ogren, W.L.2
  • 42
    • 0020376428 scopus 로고
    • Biochemical and genetic analysis of an RuBP carboxylase/ oxygenase-deficient mutant and revenants of Chlamydomonas reinhardtii
    • Spreitzer, R. J., Jordan, D. B., and Ogren, W. L. (1982) Biochemical and genetic analysis of an RuBP carboxylase/ oxygenase-deficient mutant and revenants of Chlamydomonas reinhardtii, FEBS Lett. 148, 117-121.
    • (1982) FEBS Lett. , vol.148 , pp. 117-121
    • Spreitzer, R.J.1    Jordan, D.B.2    Ogren, W.L.3
  • 43
    • 0018215519 scopus 로고
    • 14C]ribulose 1,5-bisphosphate
    • 14C]ribulose 1,5-bisphosphate, Biochem. J. 175, 909-912.
    • (1978) Biochem. J. , vol.175 , pp. 909-912
    • Kuehn, G.D.1    Hsu, T.C.2
  • 44
    • 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
  • 45
    • 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
  • 46
    • 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
  • 47
    • 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
  • 48
    • 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, 448-455.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 448-455
    • Perrakis, A.1    Sixma, T.K.2    Wilson, K.S.3    Lamzin, V.S.4
  • 49
    • 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
  • 50
    • 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
  • 51
    • 0029411262 scopus 로고
    • Occluded molecular surface: Analysis of protein packing
    • Pattabiraman, N., Ward, K. B., and Fleming, P. J. (1995) Occluded molecular surface: Analysis of protein packing, J. Mol. Recognit. 8, 334-344.
    • (1995) J. Mol. Recognit. , vol.8 , pp. 334-344
    • Pattabiraman, N.1    Ward, K.B.2    Fleming, P.J.3
  • 52
    • 0001712924 scopus 로고
    • Nonsense mutations in the Chlamydomonas chloroplast gene that codes for the large subunit of ribulosebisphosphate carboxylase/oxygenase
    • Spreitzer, R. J., Goldschmidt-Clermont, M., Rahire, M., and Rochaix, J. D. (1985) Nonsense mutations in the Chlamydomonas chloroplast gene that codes for the large subunit of ribulosebisphosphate carboxylase/oxygenase, Proc. Natl. Acad. Sci. U.S.A. 82, 5460-5464.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 5460-5464
    • Spreitzer, R.J.1    Goldschmidt-Clermont, M.2    Rahire, M.3    Rochaix, J.D.4
  • 53
    • 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
  • 54
    • 0030777759 scopus 로고    scopus 로고
    • The effect of point mutations on the free energy of transmembrane alpha-helix dimerization
    • Fleming, K. G., Ackerman, A. L., and Engelman, D. M. (1997) The effect of point mutations on the free energy of transmembrane alpha-helix dimerization, J. Mol. Biol. 272, 266-275.
    • (1997) J. Mol. Biol. , vol.272 , pp. 266-275
    • Fleming, K.G.1    Ackerman, A.L.2    Engelman, D.M.3
  • 55
    • 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
  • 56
    • 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
  • 57
    • 11844307195 scopus 로고    scopus 로고
    • Altered intersubunit interactions in crystal structures of catalytically compromised ribulose-1,5-bisphosphate carboxylase/ oxygenase
    • Karkehabadi, S., Taylor, T. C., Spreitzer, R. J., and Andersson, I. (2005) Altered intersubunit interactions in crystal structures of catalytically compromised ribulose-1,5-bisphosphate carboxylase/ oxygenase, Biochemistry 44, 113-120.
    • (2005) Biochemistry , vol.44 , pp. 113-120
    • Karkehabadi, S.1    Taylor, T.C.2    Spreitzer, R.J.3    Andersson, I.4


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