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Volumn 8, Issue 6, 2000, Pages 643-653

Conformations of the rhodopsin third cytoplasmic loop grafted onto bacteriorhodopsin

Author keywords

AFM; G protein:coupled receptor; Halobacterium salinarum; Molecular modeling; Purple membrane

Indexed keywords

BACTERIORHODOPSIN; RHODOPSIN;

EID: 0034660651     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00151-9     Document Type: Article
Times cited : (25)

References (51)
  • 1
    • 0032500697 scopus 로고    scopus 로고
    • Characterisation of an improved two-dimensional p22121 crystal from bovine rhodopsin
    • Krebs A., Villa C., Edwards P.C., Schertler G.F. Characterisation of an improved two-dimensional p22121 crystal from bovine rhodopsin. J. Mol. Biol. 282:1998;991-1003.
    • (1998) J. Mol. Biol. , vol.282 , pp. 991-1003
    • Krebs, A.1    Villa, C.2    Edwards, P.C.3    Schertler, G.F.4
  • 3
    • 0024744871 scopus 로고
    • Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction
    • Dencher N.A., Dresselhaus D., Zaccai G., Büldt G. Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction. Proc. Natl Acad. Sci. USA. 86:1989;7876-7879.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 7876-7879
    • Dencher, N.A.1    Dresselhaus, D.2    Zaccai, G.3    Büldt, G.4
  • 4
    • 0027439826 scopus 로고
    • Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin
    • Subramaniam S., Gerstein M., Oesterhelt D., Henderson R. Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. EMBO J. 12:1993;1-8.
    • (1993) EMBO J. , vol.12 , pp. 1-8
    • Subramaniam, S.1    Gerstein, M.2    Oesterhelt, D.3    Henderson, R.4
  • 6
    • 0027972897 scopus 로고
    • Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin
    • Steinhoff H-J., Mollaaghababa R., Altenbach C., Hideg K., Khorana H.G., Hubbell W.L. Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin. Science. 266:1994;105-107.
    • (1994) Science , vol.266 , pp. 105-107
    • Steinhoff, H.-J.1    Mollaaghababa, R.2    Altenbach, C.3    Hideg, K.4    Khorana, H.G.5    Hubbell, W.L.6
  • 7
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • Essen L., Siegert R., Lehmann W.D., Oesterhelt D. Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex. Proc. Natl Acad. Sci. USA. 95:1998;11 673-11 678.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 11673-11678
    • Essen, L.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 8
    • 0033582948 scopus 로고    scopus 로고
    • Site-directed spin-labeling reveals the orientation of the amino acid sidechains in the E-F loop of bacteriorhodopsin
    • Pfeiffer M., Rink T., Gerwert K., Oesterhelt D., Steinhoff H-J. Site-directed spin-labeling reveals the orientation of the amino acid sidechains in the E-F loop of bacteriorhodopsin. J. Mol. Biol. 287:1999;163-171.
    • (1999) J. Mol. Biol. , vol.287 , pp. 163-171
    • Pfeiffer, M.1    Rink, T.2    Gerwert, K.3    Oesterhelt, D.4    Steinhoff, H.-J.5
  • 9
    • 0002121233 scopus 로고    scopus 로고
    • Molecular dynamics simulation and EPR spectroscopy of nitroxide sidechains in bacteriorhodopsin
    • Steinhoff H-J., Müller M., Beier C., Pfeiffer M. Molecular dynamics simulation and EPR spectroscopy of nitroxide sidechains in bacteriorhodopsin. J. Mol. Liquids. 84:2000;17-27.
    • (2000) J. Mol. Liquids , vol.84 , pp. 17-27
    • Steinhoff, H.-J.1    Müller, M.2    Beier, C.3    Pfeiffer, M.4
  • 10
    • 0026780339 scopus 로고
    • Structure and function in rhodopsin. Studies of the interaction between the rhodopsin cytoplasmic domain and transducin
    • Franke R.R., Sakmar T.P., Graham R.M., Khorana H.G. Structure and function in rhodopsin. Studies of the interaction between the rhodopsin cytoplasmic domain and transducin. J. Biol. Chem. 267:1992;14 767-14 774.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14767-14774
    • Franke, R.R.1    Sakmar, T.P.2    Graham, R.M.3    Khorana, H.G.4
  • 11
    • 0029818639 scopus 로고    scopus 로고
    • Structure and function in rhodopsin. Single cysteine substitution mutants in the cytoplasmic interhelical E-F loop region show position-specific effects in transducin activation
    • Yang K., Farrens D.L., Hubbell W.L., Khorana H.G. Structure and function in rhodopsin. Single cysteine substitution mutants in the cytoplasmic interhelical E-F loop region show position-specific effects in transducin activation. Biochemistry. 35:1996;12 464-12 469.
    • (1996) Biochemistry , vol.35 , pp. 12464-12469
    • Yang, K.1    Farrens, D.L.2    Hubbell, W.L.3    Khorana, H.G.4
  • 12
    • 0030975286 scopus 로고    scopus 로고
    • Transducin-α C-terminal peptide binding site consists of C-D and E-F loops of rhodopsin
    • Acharya S., Saad Y., Karnik S.S. Transducin-α C-terminal peptide binding site consists of C-D and E-F loops of rhodopsin. J. Biol. Chem. 272:1997;6519-6524.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6519-6524
    • Acharya, S.1    Saad, Y.2    Karnik, S.S.3
  • 14
    • 0031055598 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Peptide sequences in the cytoplasmic loops of rhodopsin are intimately involved in interaction with rhodopsin kinase
    • Thurmond R.L., Creuzenet C., Reeves P.J., Khorana H.G. Structure and function in rhodopsin: peptide sequences in the cytoplasmic loops of rhodopsin are intimately involved in interaction with rhodopsin kinase. Proc. Natl Acad. Sci. USA. 94:1997;1715-1720.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 1715-1720
    • Thurmond, R.L.1    Creuzenet, C.2    Reeves, P.J.3    Khorana, H.G.4
  • 15
    • 0028017950 scopus 로고
    • Arrestin-rhodopsin interaction. Multi-site binding delineated by peptide inhibition
    • Krupnick J.G., Gurevich V.V., Schepers T., Hamm H.E., Benovic J.L. Arrestin-rhodopsin interaction. Multi-site binding delineated by peptide inhibition. J. Biol. Chem. 269:1994;3226-3232.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3226-3232
    • Krupnick, J.G.1    Gurevich, V.V.2    Schepers, T.3    Hamm, H.E.4    Benovic, J.L.5
  • 16
    • 0029818551 scopus 로고    scopus 로고
    • Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: A site-directed spin-labeling study
    • Altenbach C., Yang K., Farrens D.L., Farahbakhsh Z.T., Khorana H.G., Hubbell W.L. Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: a site-directed spin-labeling study. Biochemistry. 35:1996;12 470-12 478.
    • (1996) Biochemistry , vol.35 , pp. 12470-12478
    • Altenbach, C.1    Yang, K.2    Farrens, D.L.3    Farahbakhsh, Z.T.4    Khorana, H.G.5    Hubbell, W.L.6
  • 17
    • 0030841110 scopus 로고    scopus 로고
    • Three-dimensional structure of the cytoplasmic face of the G protein receptor rhodopsin
    • Yeagle P.L., Alderfer J.L., Albert A.D. Three-dimensional structure of the cytoplasmic face of the G protein receptor rhodopsin. Biochemistry. 36:1997;9649-9654.
    • (1997) Biochemistry , vol.36 , pp. 9649-9654
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 18
    • 0029021712 scopus 로고
    • Progress in high resolution atomic force microscopy in biology
    • Shao Z.F., Yang J. Progress in high resolution atomic force microscopy in biology. Quart. Rev. Biophys. 28:1995;195-251.
    • (1995) Quart. Rev. Biophys. , vol.28 , pp. 195-251
    • Shao, Z.F.1    Yang, J.2
  • 19
    • 0030951962 scopus 로고    scopus 로고
    • High resolution imaging of native biological sample surfaces using scanning probe microscopy
    • Engel A., Schoenenberger C-A., Müller D.J. High resolution imaging of native biological sample surfaces using scanning probe microscopy. Curr. Opin. Struct. Biol. 7:1997;279-284.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 279-284
    • Engel, A.1    Schoenenberger, C.-A.2    Müller, D.J.3
  • 20
    • 17344389221 scopus 로고    scopus 로고
    • Charting the surfaces of the purple membrane
    • Heymann J.B., Engel A.et al. Charting the surfaces of the purple membrane. J. Struct. Biol. 128:1999;243-249.
    • (1999) J. Struct. Biol. , vol.128 , pp. 243-249
    • Heymann, J.B.1    Engel, A.2
  • 21
    • 85047691150 scopus 로고
    • Refolding of bacteriorhodopsin. Protease V8 fragmentation and chromophore reconstitution from proteolytic V8 fragments
    • Sigrist H., Wenger R.H., Kislig E., Wüthrich M. Refolding of bacteriorhodopsin. Protease V8 fragmentation and chromophore reconstitution from proteolytic V8 fragments. Eur. J. Biochem. 177:1988;125-133.
    • (1988) Eur. J. Biochem. , vol.177 , pp. 125-133
    • Sigrist, H.1    Wenger, R.H.2    Kislig, E.3    Wüthrich, M.4
  • 22
    • 0040298977 scopus 로고    scopus 로고
    • Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane
    • Müller D.J., Sass H-J., Müller S., Büldt G., Engel A. Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane. J. Mol. Biol. 285:1999;1903-1909.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1903-1909
    • Müller, D.J.1    Sass, H.-J.2    Müller, S.3    Büldt, G.4    Engel, A.5
  • 24
    • 0039114981 scopus 로고    scopus 로고
    • Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscopy
    • Müller D.J., Fotiadis D., Scheuring S., Müller S.A., Engel A. Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscopy. Biophys. J. 76:1999;1101-1111.
    • (1999) Biophys. J. , vol.76 , pp. 1101-1111
    • Müller, D.J.1    Fotiadis, D.2    Scheuring, S.3    Müller, S.A.4    Engel, A.5
  • 25
    • 0028998339 scopus 로고
    • Force-induced conformational change of bacteriorhodopsin
    • Müller D.J., Büldt G., Engel A. Force-induced conformational change of bacteriorhodopsin. J. Mol. Biol. 249:1995;239-243.
    • (1995) J. Mol. Biol. , vol.249 , pp. 239-243
    • Müller, D.J.1    Büldt, G.2    Engel, A.3
  • 26
    • 0033567092 scopus 로고    scopus 로고
    • Protein, lipid and water organization in bacteriorhodopsin: A molecular view of the purple membrane at 1.9 Å resolution
    • Belrhali H., Pebay-Peyroula E.et al. Protein, lipid and water organization in bacteriorhodopsin: a molecular view of the purple membrane at 1.9 Å resolution. Structure. 7:1999;909-917.
    • (1999) Structure , vol.7 , pp. 909-917
    • Belrhali, H.1    Pebay-Peyroula, E.2
  • 27
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G. WHAT IF: A molecular modeling and drug design program. J. Mol. Graph. 8:1990;52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 31
    • 0021338738 scopus 로고
    • Regeneration of native bacteriorhodopsin structure from fragments
    • Liao M-J., Huang K-S., Khorana H.G. Regeneration of native bacteriorhodopsin structure from fragments. J. Biol. Chem. 259:1984;4200-4204.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4200-4204
    • Liao, M.-J.1    Huang, K.-S.2    Khorana, H.G.3
  • 32
    • 0027026810 scopus 로고
    • Bacteriorhodopsin reconstituted from two individual helices and the complementary five-helix fragment is photoactive
    • Kataoka M., Kahn T.W., Tsujiuchi Y., Engelman D.M., Tokunaga F. Bacteriorhodopsin reconstituted from two individual helices and the complementary five-helix fragment is photoactive. Photochem. Photobiol. 56:1992;895-901.
    • (1992) Photochem. Photobiol. , vol.56 , pp. 895-901
    • Kataoka, M.1    Kahn, T.W.2    Tsujiuchi, Y.3    Engelman, D.M.4    Tokunaga, F.5
  • 33
    • 0031565726 scopus 로고    scopus 로고
    • An α-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    • Baldwin J.M., Schertler G.F., Unger V.M. An α-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors. J. Mol. Biol. 272:1997;144-164.
    • (1997) J. Mol. Biol. , vol.272 , pp. 144-164
    • Baldwin, J.M.1    Schertler, G.F.2    Unger, V.M.3
  • 34
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens D.L., Altenbach C., Yang K., Hubbell W.L., Khorana H.G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science. 274:1996;768-770.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 35
    • 0030793446 scopus 로고    scopus 로고
    • Mechanism of quenching of phototransduction. Binding competition between arrestin and transducin for phosphorhodopsin
    • Krupnick J.G., Gurevich V.V., Benovic J.L. Mechanism of quenching of phototransduction. Binding competition between arrestin and transducin for phosphorhodopsin. J. Biol. Chem. 272:1997;18 125-18 131.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18125-18131
    • Krupnick, J.G.1    Gurevich, V.V.2    Benovic, J.L.3
  • 36
    • 0024980904 scopus 로고
    • Genetic transfer of the pigment bacteriorhodopsin into the eukaryote Schizosaccharomyces pombe
    • Hildebrandt V., Büldt G.et al. Genetic transfer of the pigment bacteriorhodopsin into the eukaryote Schizosaccharomyces pombe. FEBS Let. 243:1989;137-140.
    • (1989) FEBS Let. , vol.243 , pp. 137-140
    • Hildebrandt, V.1    Büldt, G.2
  • 38
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fraction into red and purple membrane
    • Oesterhelt D., Stoeckenius W. Isolation of the cell membrane of Halobacterium halobium and its fraction into red and purple membrane. Meth. Enzymol. 31:1974;667-678.
    • (1974) Meth. Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 39
    • 0030561197 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry of genetically and chemically modified bacteriorhodopsins
    • Hufnagel P., Schweiger U., Eckerskorn C., Oesterhelt D. Electrospray ionization mass spectrometry of genetically and chemically modified bacteriorhodopsins. Anal. Biochem. 243:1996;46-54.
    • (1996) Anal. Biochem. , vol.243 , pp. 46-54
    • Hufnagel, P.1    Schweiger, U.2    Eckerskorn, C.3    Oesterhelt, D.4
  • 40
    • 0026499357 scopus 로고
    • Has negative stain still a place in biomacromolecular electron microscopy?
    • Bremer A., Henn C., Engel A., Baumeister W., Aebi U. Has negative stain still a place in biomacromolecular electron microscopy? Ultramicr. 46:1992;85-111.
    • (1992) Ultramicr. , vol.46 , pp. 85-111
    • Bremer, A.1    Henn, C.2    Engel, A.3    Baumeister, W.4    Aebi, U.5
  • 41
    • 0037923070 scopus 로고    scopus 로고
    • The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions
    • Müller D.J., Engel A. The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions. Biophys. J. 73:1997;1633-1644.
    • (1997) Biophys. J. , vol.73 , pp. 1633-1644
    • Müller, D.J.1    Engel, A.2
  • 43
    • 84918249181 scopus 로고
    • The transition metal dichalcogenides discussion and interpretation of the observed optical, electrical and structural properties
    • Wilson J.A., Yoffe A.D. The transition metal dichalcogenides discussion and interpretation of the observed optical, electrical and structural properties. Advanc. Phys. 18:1969;193-335.
    • (1969) Advanc. Phys. , vol.18 , pp. 193-335
    • Wilson, J.A.1    Yoffe, A.D.2
  • 44
    • 0018650401 scopus 로고
    • Digital image processing: The semper system
    • Saxton W.O., Pitt T.J., Horner M. Digital image processing: the semper system. Ultramicr. 4:1979;343-354.
    • (1979) Ultramicr. , vol.4 , pp. 343-354
    • Saxton, W.O.1    Pitt, T.J.2    Horner, M.3
  • 45
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial cell envelope protein
    • Saxton W.O., Baumeister W. The correlation averaging of a regularly arranged bacterial cell envelope protein. J. Microsc. 127:1982;127-138.
    • (1982) J. Microsc. , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 46
    • 0021119424 scopus 로고
    • Three-dimensional reconstruction of imperfect two-dimensional crystals
    • Saxton W.O., Baumeister W., Hahn M. Three-dimensional reconstruction of imperfect two-dimensional crystals. Ultramicr. 13:1984;57-70.
    • (1984) Ultramicr. , vol.13 , pp. 57-70
    • Saxton, W.O.1    Baumeister, W.2    Hahn, M.3
  • 47
    • 84985224954 scopus 로고
    • Classification of images of biomolecular assemblies: A study of ribosomes and ribosomal subunits of Escherichia coli
    • Frank J., Bretaudiere J-P., Carazo J-M., Veschoor A., Wagenknecht T. Classification of images of biomolecular assemblies: a study of ribosomes and ribosomal subunits of Escherichia coli. J. Microsc. 150:1987;99-115.
    • (1987) J. Microsc. , vol.150 , pp. 99-115
    • Frank, J.1    Bretaudiere, J.-P.2    Carazo, J.-M.3    Veschoor, A.4    Wagenknecht, T.5
  • 48
    • 0028020713 scopus 로고
    • Reproducible acquisition of Escherichia coli porin surface topographs by atomic force microscopy
    • Schabert F.A., Engel A. Reproducible acquisition of Escherichia coli porin surface topographs by atomic force microscopy. Biophys. J. 67:1994;2394-2403.
    • (1994) Biophys. J. , vol.67 , pp. 2394-2403
    • Schabert, F.A.1    Engel, A.2
  • 49
    • 0023067967 scopus 로고
    • A new resolution criterion based on spectral signal-to-noise ratios
    • Unser M., Trus B.L., Steven A.C. A new resolution criterion based on spectral signal-to-noise ratios. Ultramicr. 23:1987;39-52.
    • (1987) Ultramicr. , vol.23 , pp. 39-52
    • Unser, M.1    Trus, B.L.2    Steven, A.C.3
  • 50
    • 0032803449 scopus 로고    scopus 로고
    • Visualizing 3D data obtained from microscopy on the Internet
    • Pittet J-J., Henn C., Engel A., Heymann J.B. Visualizing 3D data obtained from microscopy on the Internet. J. Struct. Biol. 125:1999;123-132.
    • (1999) J. Struct. Biol. , vol.125 , pp. 123-132
    • Pittet, J.-J.1    Henn, C.2    Engel, A.3    Heymann, J.B.4
  • 51
    • 0030501419 scopus 로고    scopus 로고
    • Use of noncrystallographic symmetry in protein structure refinement
    • Kleywegt G.J. Use of noncrystallographic symmetry in protein structure refinement. Acta Crystallogr. D. 52:1996;842-857.
    • (1996) Acta Crystallogr. D , vol.52 , pp. 842-857
    • Kleywegt, G.J.1


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