메뉴 건너뛰기




Volumn 378, Issue 1, 2004, Pages 45-51

The parsley plastocyanin-turnip cytochrome f complex: A structurally distorted but kinetically functional acidic patch

Author keywords

Cytochrome f; Docking; Electron transfer; NMR; Plastocyanin; Protein interaction

Indexed keywords

ELECTROSTATICS; IONIC STRENGTH; NUCLEAR MAGNETIC RESONANCE; PROTEINS; SPECTROSCOPIC ANALYSIS;

EID: 1542374666     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031423     Document Type: Article
Times cited : (22)

References (42)
  • 1
    • 0034598395 scopus 로고    scopus 로고
    • Electron transfers amongst cytochrome f, plastocyanin and Photosystem I: Kinetics and mechanisms
    • Hope, A. B. (2000) Electron transfers amongst cytochrome f, plastocyanin and Photosystem I: kinetics and mechanisms. Biochim. Biophys. Acta 1456, 5-26
    • (2000) Biochim. Biophys. Acta , vol.1456 , pp. 5-26
    • Hope, A.B.1
  • 2
    • 0027193825 scopus 로고
    • Engineering type-1 copper sites in proteins
    • Canters, G. W. and Gilardi, G. (1993) Engineering type-1 copper sites in proteins. FEBS Lett. 325, 39-48
    • (1993) FEBS Lett. , vol.325 , pp. 39-48
    • Canters, G.W.1    Gilardi, G.2
  • 3
    • 0021104996 scopus 로고
    • Structure of oxidized poplar plastocyanin at 1.6 Å resolution
    • Guss, J. M. and Freeman, H. C. (1983) Structure of oxidized poplar plastocyanin at 1.6 Å resolution. J. Mol. Biol. 169, 521-563
    • (1983) J. Mol. Biol. , vol.169 , pp. 521-563
    • Guss, J.M.1    Freeman, H.C.2
  • 4
    • 0002591183 scopus 로고    scopus 로고
    • Interprotein electron transfer
    • Bendall, D. S., ed., Bios Scientific, Oxford
    • Bendall, D. S. (1996) Interprotein electron transfer. In Protein Electron Transfer (Bendall, D. S., ed.), pp. 43-68, Bios Scientific, Oxford
    • (1996) Protein Electron Transfer , pp. 43-68
    • Bendall, D.S.1
  • 5
    • 0002305987 scopus 로고    scopus 로고
    • Protein-protein complexes formed by electron-transfer proteins
    • Kleanthous, C., ed., Oxford University Press, New York
    • Mathews, F. S., Mauk, A. G. and Moore, G. R. (2000) Protein-protein complexes formed by electron-transfer proteins. In Protein-Protein Recognition (Kleanthous, C., ed.), pp. 60-101, Oxford University Press, New York
    • (2000) Protein-Protein Recognition , pp. 60-101
    • Mathews, F.S.1    Mauk, A.G.2    Moore, G.R.3
  • 6
    • 0029995705 scopus 로고    scopus 로고
    • The role of acidic residues of plastocyanin in its interaction with cytochrome f
    • Kannt, A., Young, S. and Bendall, D. S. (1996) The role of acidic residues of plastocyanin in its interaction with cytochrome f. Biochim. Biophys. Acta 1277, 115-126
    • (1996) Biochim. Biophys. Acta , vol.1277 , pp. 115-126
    • Kannt, A.1    Young, S.2    Bendall, D.S.3
  • 7
    • 0034039797 scopus 로고    scopus 로고
    • Electrostatic aspects of protein-protein interactions
    • Sheinerman, F. B., Norel, R. and Honig, B. (2000) Electrostatic aspects of protein-protein interactions. Curr. Opin. Struct. Biol. 10, 153-159
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 153-159
    • Sheinerman, F.B.1    Norel, R.2    Honig, B.3
  • 8
    • 0142213304 scopus 로고    scopus 로고
    • Close encounters of the transient kind: Protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy
    • Crowley, P. B. and Ubbink, M. (2003) Close encounters of the transient kind: protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy. Acc. Chem. Res. 36, 723-730
    • (2003) Acc. Chem. Res. , vol.36 , pp. 723-730
    • Crowley, P.B.1    Ubbink, M.2
  • 9
    • 0034049350 scopus 로고    scopus 로고
    • Kinetics of desolvation mediated protein-protein binding
    • Camacho, C. J., Kimura, S. R., DeLisi, C. and Vajda, S. (2000) Kinetics of desolvation mediated protein-protein binding. Biophys. J. 78, 1094-1105
    • (2000) Biophys. J. , vol.78 , pp. 1094-1105
    • Camacho, C.J.1    Kimura, S.R.2    DeLisi, C.3    Vajda, S.4
  • 10
    • 0037446505 scopus 로고    scopus 로고
    • Relation between interface properties and kinetics of electron transfer in the interaction of cytochrome f and plastocyanin from plants and the cyanobacterium Phormidium laminosum
    • Schlarb-Ridley, B. G., Bendall, D. S. and Howe, C. J. (2003) Relation between interface properties and kinetics of electron transfer in the interaction of cytochrome f and plastocyanin from plants and the cyanobacterium Phormidium laminosum. Biochemistry 42, 4057-4063
    • (2003) Biochemistry , vol.42 , pp. 4057-4063
    • Schlarb-Ridley, B.G.1    Bendall, D.S.2    Howe, C.J.3
  • 12
    • 0038470801 scopus 로고    scopus 로고
    • Transient protein interactions studied by NMR spectroscopy: The case of cytochrome c and adrenodoxin
    • Worrall, J. A. R., Reinle, W., Bernhardt, R. and Ubbink, M. (2003) Transient protein interactions studied by NMR spectroscopy: the case of cytochrome c and adrenodoxin. Biochemistry 42, 7068-7076
    • (2003) Biochemistry , vol.42 , pp. 7068-7076
    • Worrall, J.A.R.1    Reinle, W.2    Bernhardt, R.3    Ubbink, M.4
  • 13
    • 0031732147 scopus 로고    scopus 로고
    • Crystal structure of spinach plastocyanin at 1.7 Å resolution
    • Xue, Y., Okvist, M., Hansson, Ö. and Young, S. (1998) Crystal structure of spinach plastocyanin at 1.7 Å resolution. Protein Sci. 7, 2099-2105
    • (1998) Protein Sci. , vol.7 , pp. 2099-2105
    • Xue, Y.1    Okvist, M.2    Hansson, Ö.3    Young, S.4
  • 16
    • 0027263613 scopus 로고
    • Importance of protein rearrangement in the electron transfer reaction between the physiological partners cytochrome f and plastocyanin
    • Qin, L. and Kostic, N. M. (1993) Importance of protein rearrangement in the electron transfer reaction between the physiological partners cytochrome f and plastocyanin. Biochemistry 32, 6073-6080
    • (1993) Biochemistry , vol.32 , pp. 6073-6080
    • Qin, L.1    Kostic, N.M.2
  • 18
    • 0026411154 scopus 로고
    • Copper protein structures
    • Adman, E. T. (1991) Copper protein structures. Adv. Protein Chem. 42, 145-197
    • (1991) Adv. Protein Chem. , vol.42 , pp. 145-197
    • Adman, E.T.1
  • 19
    • 0026796047 scopus 로고
    • Reactivity of cytochrome c and cytochrome f with mutant forms of spinach plastocyanin
    • Modi, S., Nordling, M., Lundberg, L. G., Hansson, Ö. and Bendall, D. S. (1992) Reactivity of cytochrome c and cytochrome f with mutant forms of spinach plastocyanin. Biochim. Biophys. Acta 1102, 85-90
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 85-90
    • Modi, S.1    Nordling, M.2    Lundberg, L.G.3    Hansson, Ö.4    Bendall, D.S.5
  • 21
    • 0032520957 scopus 로고    scopus 로고
    • The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics
    • Ubbink, M., Ejdebäck, M., Karlsson, B. G. and Bendall, D. S. (1998) The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics. Structure 6, 323-335
    • (1998) Structure , vol.6 , pp. 323-335
    • Ubbink, M.1    Ejdebäck, M.2    Karlsson, B.G.3    Bendall, D.S.4
  • 22
  • 23
    • 0028283635 scopus 로고
    • High-resolution solution structure of reduced parsley plastocyanin
    • Bagby, S., Driscoll, P. C., Harvey, T. S. and Hill, H. A. O. (1994) High-resolution solution structure of reduced parsley plastocyanin. Biochemistry 33, 6611-6622
    • (1994) Biochemistry , vol.33 , pp. 6611-6622
    • Bagby, S.1    Driscoll, P.C.2    Harvey, T.S.3    Hill, H.A.O.4
  • 24
    • 0035862616 scopus 로고    scopus 로고
    • Effect of pH on the self-exchange reactivity of the plant plastocyanin from parsley
    • Hunter, D. M., McFarlane, W., Sykes, A. G. and Dennison, C. (2001) Effect of pH on the self-exchange reactivity of the plant plastocyanin from parsley. Inorg. Chem. 40, 354-360
    • (2001) Inorg. Chem. , vol.40 , pp. 354-360
    • Hunter, D.M.1    McFarlane, W.2    Sykes, A.G.3    Dennison, C.4
  • 25
    • 0242600586 scopus 로고    scopus 로고
    • Active-site structure and electron-transfer reactivity of plastocyanins
    • Sato, K., Kohzuma, T. and Dennison, C. (2003) Active-site structure and electron-transfer reactivity of plastocyanins. J. Am. Chem. Soc. 125, 2101-2112
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2101-2112
    • Sato, K.1    Kohzuma, T.2    Dennison, C.3
  • 26
    • 0029897140 scopus 로고    scopus 로고
    • The heme redox center of chloroplast cytochrome f is linked to a buried five-water chain
    • Martinez, S. E., Huang, D., Ponomarev, M., Cramer, W. A. and Smith, J. L (1996) The heme redox center of chloroplast cytochrome f is linked to a buried five-water chain. Protein Sci. 5, 1081-1092
    • (1996) Protein Sci. , vol.5 , pp. 1081-1092
    • Martinez, S.E.1    Huang, D.2    Ponomarev, M.3    Cramer, W.A.4    Smith, J.L.5
  • 27
    • 0345832301 scopus 로고    scopus 로고
    • ClusPro: An automated docking and discrimination method for the prediction of protein complexes
    • Comeau, S. R., Gatchell, D. W., Vajda, S. and Camacho, C. J. (2004) ClusPro: an automated docking and discrimination method for the prediction of protein complexes. Bioinformatics 20, 45-50
    • (2004) Bioinformatics , vol.20 , pp. 45-50
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 28
    • 0038359596 scopus 로고    scopus 로고
    • Successful discrimination of protein interactions
    • Camacho, C. J. and Gatchell, D. W. (2003) Successful discrimination of protein interactions. Proteins 52, 92-97
    • (2003) Proteins , vol.52 , pp. 92-97
    • Camacho, C.J.1    Gatchell, D.W.2
  • 31
    • 0037080005 scopus 로고    scopus 로고
    • Unusual properties of plastocyanin from the fern Dryopteris crassirhizoma
    • Dennison, C., Lawler, A. T. and Kohzuma, T. (2002) Unusual properties of plastocyanin from the fern Dryopteris crassirhizoma. Biochemistry 41, 552-560
    • (2002) Biochemistry , vol.41 , pp. 552-560
    • Dennison, C.1    Lawler, A.T.2    Kohzuma, T.3
  • 32
    • 0039591353 scopus 로고    scopus 로고
    • Side-chain interactions in the plastocyanin-cytochrome f complex
    • Ejdebäck, M., Bergkvist, A., Karlsson, B. G. and Ubbink, M. (2000) Side-chain interactions in the plastocyanin-cytochrome f complex. Biochemistry 39, 5022-5027
    • (2000) Biochemistry , vol.39 , pp. 5022-5027
    • Ejdebäck, M.1    Bergkvist, A.2    Karlsson, B.G.3    Ubbink, M.4
  • 33
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • Zuiderweg, E. R. P (2002) Mapping protein-protein interactions in solution by NMR spectroscopy. Biochemistry 41, 1-7
    • (2002) Biochemistry , vol.41 , pp. 1-7
    • Zuiderweg, E.R.P.1
  • 34
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling
    • Guex, N. and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling. Electrophoresis 18, 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 35
    • 0034255358 scopus 로고    scopus 로고
    • DbClustal: Rapid and reliable global multiple alignments of protein sequences detected by database searches
    • Thompson, J. D., Plewniak, F., Thierry, J. C. and Poch, O. (2000) DbClustal: rapid and reliable global multiple alignments of protein sequences detected by database searches. Nucleic Acids Res. 28, 2919-2926
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2919-2926
    • Thompson, J.D.1    Plewniak, F.2    Thierry, J.C.3    Poch, O.4
  • 37
    • 0346319014 scopus 로고    scopus 로고
    • Plastocyanin-cytochrome f interactions: The influence of hydrophobic patch mutations studied by NMR spectroscopy
    • Crowley, P. B., Vintonenko, N., Bullerjahn, G. S. and Ubbink, M. (2002) Plastocyanin-cytochrome f interactions: the influence of hydrophobic patch mutations studied by NMR spectroscopy. Biochemistry 41, 15698-15705
    • (2002) Biochemistry , vol.41 , pp. 15698-15705
    • Crowley, P.B.1    Vintonenko, N.2    Bullerjahn, G.S.3    Ubbink, M.4
  • 38
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte, L., Chothia, C. and Janin, J. (1999) The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285, 2177-2198
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 39
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan, A. A. and Thorn, K. S. (1998) Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280, 1-9
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 41
    • 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. Cryst. 24, 946-950
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 42
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.