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Volumn 428, Issue 6980, 2004, Pages 287-292

Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution

Author keywords

[No Author keywords available]

Indexed keywords

CHLOROPHYLL; HARVESTING; PLANTS (BOTANY); SOLAR ENERGY;

EID: 1642602038     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02373     Document Type: Article
Times cited : (1458)

References (42)
  • 1
    • 0026056608 scopus 로고
    • Biochemical composition and organization of higher plant photosystem II light-harvesting pigment-proteins
    • Peter, G. F. & Thornber, J. P. Biochemical composition and organization of higher plant photosystem II light-harvesting pigment-proteins. J. Biol. Chem. 266, 16745-16754 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 16745-16754
    • Peter, G.F.1    Thornber, J.P.2
  • 2
    • 0033537961 scopus 로고    scopus 로고
    • Determination of the stoichiometry and strength of binding of xanthophylls to the photosystem II light harvesting complexes
    • Ruban, A. V., Lee, P. J., Wentworth, M., Young, A. J. & Horton, P. Determination of the stoichiometry and strength of binding of xanthophylls to the photosystem 11 light harvesting complexes. J. Biol. Chem. 274, 10458-10465 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 10458-10465
    • Ruban, A.V.1    Lee, P.J.2    Wentworth, M.3    Young, A.J.4    Horton, P.5
  • 3
    • 0027452052 scopus 로고
    • Lipid-protein interactions in crystals of plant light-harvesting complex
    • Nußberger, S., Dörr, K., Wang, D. N. & Kühlbrandt, W. Lipid-protein interactions in crystals of plant light-harvesting complex. J. Mol. Biol. 234, 347-356 (1993).
    • (1993) J. Mol. Biol. , vol.234 , pp. 347-356
    • Nußberger, S.1    Dörr, K.2    Wang, D.N.3    Kühlbrandt, W.4
  • 5
    • 0036672384 scopus 로고    scopus 로고
    • A major light-harvesting polypeptide of photosystem 11 functions in thermal dissipation
    • Elrad, D., Niyogi, K. K. Grossman, A. R. A major light-harvesting polypeptide of photosystem 11 functions in thermal dissipation. Plant Cell 14, 1801-1816 (2002).
    • (2002) Plant Cell , vol.14 , pp. 1801-1816
    • Elrad, D.1    Niyogi, K.K.2    Grossman, A.R.3
  • 6
    • 0030794462 scopus 로고    scopus 로고
    • Phosphorylation controls the three-dimensional structure of plant light harvesting complex 11
    • Nilsson, A. et al. Phosphorylation controls the three-dimensional structure of plant light harvesting complex 11. J. Biol. Chem. 272, 18350-18357 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 18350-18357
    • Nilsson, A.1
  • 7
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt, W., Wang, D. N. & Fujiyoshi, Y. Atomic model of plant light-harvesting complex by electron crystallography. Nature 367, 614-621 (1994).
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 8
    • 0001791586 scopus 로고
    • Crystallization of membrane proteins
    • Michel, H. Crystallization of membrane proteins. Trends Biochem. Sci. 8, 56-59 (1983).
    • (1983) Trends Biochem. Sci. , vol.8 , pp. 56-59
    • Michel, H.1
  • 10
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • Jordan, P. et al. Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 411, 909-917 (2001).
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1
  • 11
    • 0035979355 scopus 로고    scopus 로고
    • The crystallographic structure of the B800-820 LH3 light-harvesting complex from the purple bacteria Rhodopseudomonas acidophila strain 7050
    • McLuskey, K., Prince, S. M., Cogdell, R. J. & Isaacs, N. W. The crystallographic structure of the B800-820 LH3 light-harvesting complex from the purple bacteria Rhodopseudomonas acidophila strain 7050. Biochemistry 40, 8783-8789 (2001).
    • (2001) Biochemistry , vol.40 , pp. 8783-8789
    • McLuskey, K.1    Prince, S.M.2    Cogdell, R.J.3    Isaacs, N.W.4
  • 12
    • 0033621082 scopus 로고    scopus 로고
    • Mutational analysis of a higher plant antenna protein provides identification of chromophores bound into multiple sites
    • Bassi, R., Croce, R., Cugini, D. & Sandonà, D. Mutational analysis of a higher plant antenna protein provides identification of chromophores bound into multiple sites. Proc. Natl Acad. Sci. USA 96, 10056-10061 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10056-10061
    • Bassi, R.1    Croce, R.2    Cugini, D.3    Sandonà, D.4
  • 13
    • 0033584940 scopus 로고    scopus 로고
    • Chlorophyll binding to monomeric light-harvesting complex. A mutation analysis of chromophore-binding residues
    • Remelli, R., Varotto, C., Sandonà, D., Croce, R. & Bassi, R. Chlorophyll binding to monomeric light-harvesting complex. A mutation analysis of chromophore-binding residues. J. Biol. Chem. 274, 33510-33521 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 33510-33521
    • Remelli, R.1    Varotto, C.2    Sandonà, D.3    Croce, R.4    Bassi, R.5
  • 14
    • 0031794854 scopus 로고    scopus 로고
    • The flow of excitation energy in LHCII monomers: Implications for the structural model of the major plant antenna
    • Gradinaru, C. C. et al. The flow of excitation energy in LHCII monomers: implications for the structural model of the major plant antenna. Biophys. J. 75, 3064-3077 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 3064-3077
    • Gradinaru, C.C.1
  • 15
    • 0030870674 scopus 로고    scopus 로고
    • Novel aspects of chlorophyll a/b-binding proteins
    • Bassi, R., Sandonà, D. & Croce, R. Novel aspects of chlorophyll a/b-binding proteins. Physiol. Planta. 100, 769-779 (1997).
    • (1997) Physiol. Planta. , vol.100 , pp. 769-779
    • Bassi, R.1    Sandonà, D.2    Croce, R.3
  • 16
    • 0000683917 scopus 로고
    • Reconstitution of chlorophyll a/b light-harvesting complexes: Xanthophyll-dependent assembly and energy transfer
    • Plumley, F. G. & Schmidt, G. W. Reconstitution of chlorophyll a/b light-harvesting complexes: Xanthophyll-dependent assembly and energy transfer. Proc. Natl Acad. Sci. USA 84, 146-150 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 146-150
    • Plumley, F.G.1    Schmidt, G.W.2
  • 17
    • 0033569933 scopus 로고    scopus 로고
    • Carotenoid-binding sites of the major light-harvesting complex II of higher plants
    • Croce, R., Weiss, S. & Bassi, R. Carotenoid-binding sites of the major light-harvesting complex II of higher plants. J. Biol. Chem. 274, 29613-29623 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 29613-29623
    • Croce, R.1    Weiss, S.2    Bassi, R.3
  • 18
    • 0027301940 scopus 로고
    • Pigments induce folding of light-harvesting chlorophyll a/b-binding protein
    • Paulsen, H., Finkenzeller, B. & Kuhlein, N. Pigments induce folding of light-harvesting chlorophyll a/b-binding protein. Eur. J. Biochem. 215, 809-816 (1993).
    • (1993) Eur. J. Biochem. , vol.215 , pp. 809-816
    • Paulsen, H.1    Finkenzeller, B.2    Kuhlein, N.3
  • 19
    • 0001305233 scopus 로고    scopus 로고
    • Carotenoid binding sites in LHCIIb. Relative affinities towards major xanthophylls of higher plants
    • Hobe, S., Niemeier, H., Bender, A. & Paulsen, H. Carotenoid binding sites in LHCIIb. Relative affinities towards major xanthophylls of higher plants. Eur. J. Biochem. 267, 616-624 (2000).
    • (2000) Eur. J. Biochem. , vol.267 , pp. 616-624
    • Hobe, S.1    Niemeier, H.2    Bender, A.3    Paulsen, H.4
  • 20
    • 0032769733 scopus 로고    scopus 로고
    • The neoxanthin binding site of the major light harvesting complex (LHCII) from higher plants
    • Croce, R., Remelli, R., Varotto, C., Breton, J. & Bassi, R. The neoxanthin binding site of the major light harvesting complex (LHCII) from higher plants. FEBS Lett. 456, 1-6 (1999).
    • (1999) FEBS Lett. , vol.456 , pp. 1-6
    • Croce, R.1    Remelli, R.2    Varotto, C.3    Breton, J.4    Bassi, R.5
  • 21
    • 0034300084 scopus 로고    scopus 로고
    • Identifying the pathways of energy transfer between carotenoids and chlorophylls in LHCII and CP29. A multicolor, femtosecond pump-probe study
    • Gradinaru, C. C., Stokkum, I. H. M. V., Pascal, A. A., Grondelle, R. V. & Amerongen, H. V. Identifying the pathways of energy transfer between carotenoids and chlorophylls in LHCII and CP29. A multicolor, femtosecond pump-probe study. J. Phys. Chem. B 104, 9330-9342 (2000).
    • (2000) J. Phys. Chem. B , vol.104 , pp. 9330-9342
    • Gradinaru, C.C.1    Stokkum, I.H.M.V.2    Pascal, A.A.3    Grondelle, R.V.4    Amerongen, H.V.5
  • 22
    • 0035144442 scopus 로고    scopus 로고
    • Carotenoid-to-chlorophyll energy transfer in recombinant major light-harvesting complex (LHC-II) of higher plants. I. Femtosecond transient absorption measurements
    • Croce, R., Müller, M. G., Bassi, R. & Holzwarth, A. R. Carotenoid-to-chlorophyll energy transfer in recombinant major light-harvesting complex (LHC-II) of higher plants. I. femtosecond transient absorption measurements. Biophys. J. 80, 901-915 (2001).
    • (2001) Biophys. J. , vol.80 , pp. 901-915
    • Croce, R.1    Müller, M.G.2    Bassi, R.3    Holzwarth, A.R.4
  • 23
    • 0034684163 scopus 로고    scopus 로고
    • Plant lipocalins: Violaxanthin de-epoxidase and zeaxanthin epoxidase
    • Hieber, A. D., Bugos, R. C. & Yamamoto, H. Y. Plant lipocalins: violaxanthin de-epoxidase and zeaxanthin epoxidase. Biochim. Biophys. Acta 1482, 84-91 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 84-91
    • Hieber, A.D.1    Bugos, R.C.2    Yamamoto, H.Y.3
  • 25
    • 0030995292 scopus 로고    scopus 로고
    • Mechanistic aspects of xanthophyll cycle-dependent photoprotection in higher plant chloroplasts and leaves
    • Gilmore, A. M. Mechanistic aspects of xanthophyll cycle-dependent photoprotection in higher plant chloroplasts and leaves. Physiol. Planta. 99, 197-209 (1997).
    • (1997) Physiol. Planta. , vol.99 , pp. 197-209
    • Gilmore, A.M.1
  • 26
    • 0028156508 scopus 로고
    • Photophysics of the carotenoids associated with the xanthophyll cycle in photosynthesis
    • Frank, H. A. et al. Photophysics of the carotenoids associated with the xanthophyll cycle in photosynthesis. Photosynth. Res. 41, 389-395 (1994).
    • (1994) Photosynth. Res. , vol.41 , pp. 389-395
    • Frank, H.A.1
  • 27
    • 0037447051 scopus 로고    scopus 로고
    • Evidence for direct carotenoid involvement in the regulation of photosynthetic light harvesting
    • Ma, Y. Z., Holt, N. E., Li, X. P., Niyogi, K. K. & Fleming, G. R. Evidence for direct carotenoid involvement in the regulation of photosynthetic light harvesting. Proc. Natl Acad. Sci. USA 100, 4377-4382 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4377-4382
    • Ma, Y.Z.1    Holt, N.E.2    Li, X.P.3    Niyogi, K.K.4    Fleming, G.R.5
  • 28
    • 0005323080 scopus 로고
    • Concentration quenching of chlorophyll fluorescence in bilayer lipid vesicles and liposomes
    • Beddard, G. S., Carlin, S. E. & Porter, G. Concentration quenching of chlorophyll fluorescence in bilayer lipid vesicles and liposomes. Chem. Phys. Lett. 43, 27-32 (1976).
    • (1976) Chem. Phys. Lett. , vol.43 , pp. 27-32
    • Beddard, G.S.1    Carlin, S.E.2    Porter, G.3
  • 29
    • 0035940523 scopus 로고    scopus 로고
    • Time-resolved fluorescence analysis of the photosystem II antenna proteins in detergent micelles and liposomes
    • Moya, I., Silvestri, M., Vallon, O., Cinque, G. & Bassi, R. Time-resolved fluorescence analysis of the photosystem II antenna proteins in detergent micelles and liposomes. Biochemistry 40, 12552-12561 (2001).
    • (2001) Biochemistry , vol.40 , pp. 12552-12561
    • Moya, I.1    Silvestri, M.2    Vallon, O.3    Cinque, G.4    Bassi, R.5
  • 30
    • 0040327783 scopus 로고
    • A comparative study on PS 11 light harvesting chlorophyll a/b protein complexes between spinach and cucumber
    • Lou, S., Wang, K., Zhao, F., Xu, C. & Kuang, T. A comparative study on PS 11 light harvesting chlorophyll a/b protein complexes between spinach and cucumber. Acta Bot. Sin. 37, 192-197 (1995).
    • (1995) Acta Bot. Sin. , vol.37 , pp. 192-197
    • Lou, S.1    Wang, K.2    Zhao, F.3    Xu, C.4    Kuang, T.5
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 32
  • 33
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB v2.0
    • Weeks, C. M. & Miller, R. The design and implementation of SnB v2.0. J. Appl. Crystallogr. 32, 120-124 (1999).
    • (1999) J. Appl. Crystallogr. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 34
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 Collaborative Computational Project, The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 35
    • 0042494813 scopus 로고
    • (eds Dodson, E. J., Gover, S. & Wolf, W.) (SERC Daresbury Laboratory, Warrington)
    • Jones, T. A. in Molecular Replacement (eds Dodson, E. J., Gover, S. & Wolf, W.) 92-105 (SERC Daresbury Laboratory, Warrington, 1992).
    • (1992) Molecular Replacement , pp. 92-105
    • Jones, T.A.1
  • 36
    • 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. & Kjeldgaard, M. 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).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 37
    • 0024967180 scopus 로고
    • Nucleotide sequence of a cDNA encoding the light-harvesting chlorophyll a/b binding protein from spinach
    • Mason, J. G. Nucleotide sequence of a cDNA encoding the light-harvesting chlorophyll a/b binding protein from spinach. Nucleic Acids Res. 17, 5387 (1989).
    • (1989) Nucleic Acids Res. , vol.17 , pp. 5387
    • Mason, J.G.1
  • 38
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brünger, A. T. et al. Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 39
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (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
  • 40
    • 0029619259 scopus 로고
    • Knowledge-based secondary structure assignment
    • Frishman, D. & Argos, P. Knowledge-based secondary structure assignment. Proteins Struct. Funct. Genet. 23, 566-579 (1995).
    • (1995) Proteins Struct. Funct. Genet. , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 41
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 42
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merritt, E. A. & Murphy, M. E. P. Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D 50, 869-873 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2


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