메뉴 건너뛰기




Volumn 14, Issue 3, 2005, Pages 799-811

The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 visualized by NMR and docking using HADDOCK

Author keywords

Cytochrome b5; Cytochrome c; Docking; Electron transfer; HADDOCK; NMR

Indexed keywords

CYTOCHROME B5; CYTOCHROME C; DOCKING PROTEIN;

EID: 14144250394     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041150205     Document Type: Article
Times cited : (49)

References (53)
  • 1
    • 1842450290 scopus 로고    scopus 로고
    • A docking approach to the study of copper trafficking proteins: Interaction between metallochaperones and soluble domains of copper ATPases
    • Arnesano, F., Banci, L., Bertini, I., and Bonvin, A.M.J.J. 2004. A docking approach to the study of copper trafficking proteins: Interaction between metallochaperones and soluble domains of copper ATPases. Structure 12: 669-676.
    • (2004) Structure , vol.12 , pp. 669-676
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Bonvin, A.M.J.J.4
  • 3
    • 0026608669 scopus 로고
    • Oxidation state-dependent conformational changes in cytochrome c
    • Berghuis, A.M. and Brayer, G.D. 1992. Oxidation state-dependent conformational changes in cytochrome c. J. Mol. Biol. 233: 959-976.
    • (1992) J. Mol. Biol. , vol.233 , pp. 959-976
    • Berghuis, A.M.1    Brayer, G.D.2
  • 5
    • 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
  • 6
    • 0036903969 scopus 로고    scopus 로고
    • The ternary complex of cytochrome/and cytochrome c: Identification of a second binding site and competition for plastocyanin binding
    • Crowley, P B., Rabe, K.S., Worrall, J.A.R., Canters, G.W., and Ubbink, M. 2002. The ternary complex of cytochrome/and cytochrome c: Identification of a second binding site and competition for plastocyanin binding. Chembiochem 3: 526-533.
    • (2002) Chembiochem , vol.3 , pp. 526-533
    • Crowley, P.B.1    Rabe, K.S.2    Worrall, J.A.R.3    Canters, G.W.4    Ubbink, M.5
  • 7
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical and/or biophysical information
    • Dominguez, C., Boelens, R., and Bonvin, A.M.J.J. 2003. HADDOCK: A protein-protein docking approach based on biochemical and/or biophysical information. J. Am. Chem. Soc. 125: 1731-1737.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.J.J.3
  • 11
    • 0025370793 scopus 로고
    • Assignment of proton resonances, identification of secondary structural elements, and analysis of backbone chemical shifts for the C102T variant of yeast iso-1-cytochrome c and horse cytochrome c
    • Gao, Y., Boyd, J., Williams, R.J.P., and Pielak, G.J. 1990. Assignment of proton resonances, identification of secondary structural elements, and analysis of backbone chemical shifts for the C102T variant of yeast iso-1-cytochrome c and horse cytochrome c. Biochemistry 29: 6994-7003.
    • (1990) Biochemistry , vol.29 , pp. 6994-7003
    • Gao, Y.1    Boyd, J.2    Williams, R.J.P.3    Pielak, G.J.4
  • 12
  • 13
    • 0034515845 scopus 로고    scopus 로고
    • Ansig for Windows: An interactive computer program for semiautomatic assignment of protein NMR spectra
    • Helgstrand, M., Kraulis, P.J., Allard, P., and Hard, T. 2000. Ansig for Windows: An interactive computer program for semiautomatic assignment of protein NMR spectra. J. Biol. NMR 18: 329-336.
    • (2000) J. Biol. NMR , vol.18 , pp. 329-336
    • Helgstrand, M.1    Kraulis, P.J.2    Allard, P.3    Hard, T.4
  • 15
    • 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
  • 16
    • 0019333795 scopus 로고
    • 1 NMR lines of the heme group and selected amino acid residues
    • 1 NMR lines of the heme group and selected amino acid residues. Biochim. Biophys. Acta 621: 204-217.
    • (1980) Biochim. Biophys. Acta , vol.621 , pp. 204-217
    • Keller, R.M.1    Wüthrich, K.2
  • 17
    • 0001250026 scopus 로고
    • 1 and 2D NMR spectra by interactive computer graphics
    • 1 and 2D NMR spectra by interactive computer graphics. J. Magn. Reson. 84: 627-633.
    • (1989) J. Magn. Reson. , vol.84 , pp. 627-633
    • Kraulis, P.J.1
  • 18
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • _. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
  • 19
    • 0000693098 scopus 로고
    • Proton nuclear magnetic resonance characterization of heme disorder in hemoproteins
    • La Mar, G.N., Budd, D.L., Viscio, D.B., Smith, K.M., and Langry, K.C. 1978. Proton nuclear magnetic resonance characterization of heme disorder in hemoproteins. Proc. Natl. Acad. Sci. 75: 5755-5759.
    • (1978) Proc. Natl. Acad. Sci. , vol.75 , pp. 5755-5759
    • La Mar, G.N.1    Budd, D.L.2    Viscio, D.B.3    Smith, K.M.4    Langry, K.C.5
  • 22
    • 0025146477 scopus 로고
    • High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c
    • Louie, G.V. and Brayer, G.D. 1990. High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c. J. Mol. Biol. 214: 527-555.
    • (1990) J. Mol. Biol. , vol.214 , pp. 527-555
    • Louie, G.V.1    Brayer, G.D.2
  • 28
    • 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
  • 32
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K., and Honig, B. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11: 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 34
    • 0032574759 scopus 로고    scopus 로고
    • Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys 72 in yeast iso-1-cytochrome c and the alkaline conformational transition
    • Pollock, W.B.R., Resell, F.I., Twitchett, M.B., Dumont, M.E., and Mauk, A.G. 1998. Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys 72 in yeast iso-1-cytochrome c and the alkaline conformational transition. Biochemistry 37: 6124-6131.
    • (1998) Biochemistry , vol.37 , pp. 6124-6131
    • Pollock, W.B.R.1    Resell, F.I.2    Twitchett, M.B.3    Dumont, M.E.4    Mauk, A.G.5
  • 37
    • 1642322414 scopus 로고    scopus 로고
    • Mapping the electron transfer interface between cytochrome b5 and cytochrome c
    • Ren, Y., Wang, W.H., Wang, Y.H., Case, M., Qian, W., Mclendon, G.L., and Huang, Z.X. 2004. Mapping the electron transfer interface between cytochrome b5 and cytochrome c. Biochemistry 43: 3527-3536.
    • (2004) Biochemistry , vol.43 , pp. 3527-3536
    • Ren, Y.1    Wang, W.H.2    Wang, Y.H.3    Case, M.4    Qian, W.5    Mclendon, G.L.6    Huang, Z.X.7
  • 38
    • 0025934756 scopus 로고
    • Mapping electrostatic interactions in macromolecular associations
    • Rodgers, K.K. and Sligar, S.G. 1991. Mapping electrostatic interactions in macromolecular associations. J. Mol. Biol. 221: 1453-1460.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1453-1460
    • Rodgers, K.K.1    Sligar, S.G.2
  • 45
    • 0015803893 scopus 로고
    • The structure of ferrocytochrome c at 2.45 Å resolution
    • Takano, T., Kallai, O.B., Swanson, R., and Dickerson, R.E. 1973. The structure of ferrocytochrome c at 2.45 Å resolution. J. Biol. Chem. 248: 5234-5246.
    • (1973) J. Biol. Chem. , vol.248 , pp. 5234-5246
    • Takano, T.1    Kallai, O.B.2    Swanson, R.3    Dickerson, R.E.4
  • 47
    • 0030990022 scopus 로고    scopus 로고
    • Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis
    • Ubbink, M. and Bendall, D.S. 1997. Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis. Biochemistry 36: 6326-6335.
    • (1997) Biochemistry , vol.36 , pp. 6326-6335
    • Ubbink, M.1    Bendall, D.S.2
  • 51
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.