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Volumn 401, Issue 6755, 1999, Pages 822-826

High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN;

EID: 0033592726     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/44623     Document Type: Article
Times cited : (315)

References (32)
  • 1
    • 0015244581 scopus 로고
    • Rhodopsin-like protein from the purple membrane of Halobacterium halobium
    • Oesterhelt, D. & Stoeckenius, W. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nature New Biol. 233, 149-152 (1971).
    • (1971) Nature New Biol. , vol.233 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 2
    • 0016842810 scopus 로고
    • Three dimensional model of purple membrane obtained by electron microscopy
    • Henderson, R. & Unwin, P. N. T. Three dimensional model of purple membrane obtained by electron microscopy. Nature 257, 28-32 (1975).
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.T.2
  • 3
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
    • Landau, E. M. & Rosenbusch, J. P. Lipidic cubic phases: A novel concept for the crystallization of membrane proteins. Proc. Natl Acad. Sci. USA 93, 14532-14535 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 4
    • 0031829172 scopus 로고    scopus 로고
    • Lipidic cubic phases: New matrices for the three dimensional crystallization of membrane proteins
    • Rummel, G. et al. Lipidic cubic phases: New matrices for the three dimensional crystallization of membrane proteins. J. Struct. Biol. 121, 82-91 (1998).
    • (1998) J. Struct. Biol. , vol.121 , pp. 82-91
    • Rummel, G.1
  • 6
    • 0032510475 scopus 로고    scopus 로고
    • Structure at 0.85 Å resolution of an early protein photocycle intermediate
    • Genick, U. K., Soltis, S. M., Kuhn, P., Canestrelli, I. L. & Getzoff, E. D. Structure at 0.85 Å resolution of an early protein photocycle intermediate. Nature 392, 206-209 (1998).
    • (1998) Nature , vol.392 , pp. 206-209
    • Genick, U.K.1    Soltis, S.M.2    Kuhn, P.3    Canestrelli, I.L.4    Getzoff, E.D.5
  • 7
    • 0027728765 scopus 로고
    • A fast and portable microspectrophotometer for protein crystallography
    • Hadfield, A. & Hajdu, J. A fast and portable microspectrophotometer for protein crystallography. J. Appl. Crystallogr. 26, 839-842 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 839-842
    • Hadfield, A.1    Hajdu, J.2
  • 8
    • 33751500154 scopus 로고
    • Picosecond time-resolved resonance Raman spectroscopy of bacteriorhodopsin's J, K and KL intermediates
    • Doig, S. J., Reid, P. J. & Mathies, R. A. Picosecond time-resolved resonance Raman spectroscopy of bacteriorhodopsin's J, K and KL intermediates. J. Phys. Chem. 95, 6372-6379 (1991).
    • (1991) J. Phys. Chem. , vol.95 , pp. 6372-6379
    • Doig, S.J.1    Reid, P.J.2    Mathies, R.A.3
  • 9
    • 0025052669 scopus 로고
    • Quantum efficiencies of bacteriorhodopsin photochemical reactions
    • Xie, A. Quantum efficiencies of bacteriorhodopsin photochemical reactions. Biophys. J. 58, 1127-1132 (1990).
    • (1990) Biophys. J. , vol.58 , pp. 1127-1132
    • Xie, A.1
  • 10
    • 0033548544 scopus 로고    scopus 로고
    • The projection structure of the low temperature K intermediate of the bacteriorhodopsin photocycle determined by electron diffraction
    • Bullough, P. A. & Henderson, R. The projection structure of the low temperature K intermediate of the bacteriorhodopsin photocycle determined by electron diffraction. J. Mol. Biol. 286, 1663-1671 (1999).
    • (1999) J. Mol. Biol. , vol.286 , pp. 1663-1671
    • Bullough, P.A.1    Henderson, R.2
  • 11
    • 0020008581 scopus 로고
    • Resonance Raman spectra of bacteriorhodopsin's primary photoproduct: Evidence for a distorted 13-cis retinal chromophore
    • Braiman, M. & Mathies, R. Resonance Raman spectra of bacteriorhodopsin's primary photoproduct: Evidence for a distorted 13-cis retinal chromophore. Proc. Natl Acad. Sci. USA 79, 403-407 (1982).
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 403-407
    • Braiman, M.1    Mathies, R.2
  • 12
    • 0028019123 scopus 로고
    • Reorientations in the bacteriorhodopsin photocycle
    • Song, Q., Harms, G. S., Wan, C. & Johnson, C. K. Reorientations in the bacteriorhodopsin photocycle. Biochemistry 33, 14026-14033 (1994).
    • (1994) Biochemistry , vol.33 , pp. 14026-14033
    • Song, Q.1    Harms, G.S.2    Wan, C.3    Johnson, C.K.4
  • 13
    • 0028283324 scopus 로고
    • Active site lysine backbone undergoes conformational changes in the bacteriorhodopsin photocycle
    • Takei, H., Gat, Y., Rothman, Z., Lewis, A. & Sheves, M. Active site lysine backbone undergoes conformational changes in the bacteriorhodopsin photocycle. J. Biol. Chem. 269, 7387-7389 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 7387-7389
    • Takei, H.1    Gat, Y.2    Rothman, Z.3    Lewis, A.4    Sheves, M.5
  • 14
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution
    • Luecke, H., Richter, H. T. & Lanyi, J. K. Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution. Science 280, 1934-1937 (1998).
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.T.2    Lanyi, J.K.3
  • 15
    • 0033567092 scopus 로고    scopus 로고
    • Protein, lipid and water organization in bacteriorhodopsin crystals: A molecular view of the purple membrane at 1.9 Å resolution
    • Belrhali, H. et al. Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 Å resolution. Structure 7, 909-917 (1999).
    • (1999) Structure , vol.7 , pp. 909-917
    • Belrhali, H.1
  • 16
    • 0000559536 scopus 로고
    • A mechanism for controlling the pKa of the retinal protonated Schiff base in retinal proteins. A study with model compounds
    • Gat, Y. & Sheves, M. A mechanism for controlling the pKa of the retinal protonated Schiff base in retinal proteins. A study with model compounds. J. Am. Chem. Soc. 115, 3772-3773 (1993).
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3772-3773
    • Gat, Y.1    Sheves, M.2
  • 17
    • 0031039399 scopus 로고    scopus 로고
    • Structure of a protein photocycle intermediate by millisecond time-resolved crystallography
    • Genick, U. K. et al. Structure of a protein photocycle intermediate by millisecond time-resolved crystallography. Science 275, 1471-1475 (1997).
    • (1997) Science , vol.275 , pp. 1471-1475
    • Genick, U.K.1
  • 18
    • 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, 7876-7879 (1989).
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 7876-7879
    • Dencher, N.A.1    Dresselhaus, D.2    Zaccai, G.3    Büldt, G.4
  • 19
    • 0025976082 scopus 로고
    • Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin
    • Koch, M. H. J. et al. Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin. EMBO J. 10, 521-526 (1991).
    • (1991) EMBO J. , vol.10 , pp. 521-526
    • Koch, M.H.J.1
  • 20
    • 0026094796 scopus 로고
    • Crystallographic characterization by X-ray diffraction of the M-intermediate from the photocycle of bacteriorhodopsin at room temperature
    • Nakasako, M., Kataoka, M., Amemiva, Y. & Tokunaga, F. Crystallographic characterization by X-ray diffraction of the M-intermediate from the photocycle of bacteriorhodopsin at room temperature. FEBS Lett. 292, 73-75 (1991).
    • (1991) FEBS Lett. , vol.292 , pp. 73-75
    • Nakasako, M.1    Kataoka, M.2    Amemiva, Y.3    Tokunaga, F.4
  • 21
    • 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, 1-8 (1993).
    • (1993) EMBO J. , vol.12 , pp. 1-8
    • Subramaniam, S.1    Gerstein, M.2    Oesterhelt, D.3    Henderson, R.4
  • 22
    • 0029886089 scopus 로고    scopus 로고
    • A three-dimensional difference map of the N-intermediate in the bacteriorhodopsin photocycle: Part of the F helix tilts in the M to N transition
    • Vonck, J. A three-dimensional difference map of the N-intermediate in the bacteriorhodopsin photocycle: part of the F helix tilts in the M to N transition. Biochemistry 35, 5870-5878 (1996).
    • (1996) Biochemistry , vol.35 , pp. 5870-5878
    • Vonck, J.1
  • 23
    • 0032414367 scopus 로고    scopus 로고
    • Enzymic release of crystals from lipidic cubic phases
    • Nollert, P. & Landau, E. M. Enzymic release of crystals from lipidic cubic phases. Biochem. Soc. Trans. 26, 709-713 (1998).
    • (1998) Biochem. Soc. Trans. , vol.26 , pp. 709-713
    • Nollert, P.1    Landau, E.M.2
  • 24
    • 0002452464 scopus 로고
    • eds Sawyer, L., Isaacs, N. W. & Bailey, S. DL/SCI/ R34, Daresbury Laboratory, Warrington
    • Otwinowski, Z. in Data Collection and Processing (eds Sawyer, L., Isaacs, N. W. & Bailey, S.) DL/SCI/ R34, 55-62 (Daresbury Laboratory, Warrington, 1993).
    • (1993) Data Collection and Processing , pp. 55-62
    • Otwinowski, Z.1
  • 25
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project nr4
    • Collaborative Computational Project nr4. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 26
    • 0031059039 scopus 로고    scopus 로고
    • Detecting and overcoming crystal twinning
    • Yeates, T. O. Detecting and overcoming crystal twinning. Methods Enzymol. 276, 344-358 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 344-358
    • Yeates, T.O.1
  • 27
    • 0032552110 scopus 로고    scopus 로고
    • Structure of a cephalosporin synthase
    • Valegȧrd, K. et al. Structure of a cephalosporin synthase. Nature 394, 805-809 (1998).
    • (1998) Nature , vol.394 , pp. 805-809
    • Valegard, K.1
  • 28
    • 0001546886 scopus 로고    scopus 로고
    • Improved estimation of structure-factor difference amplitudes from poorly accurate data
    • Ursby, T. & Bourgeois, D. Improved estimation of structure-factor difference amplitudes from poorly accurate data. Acta Crystallogr. A 53, 564-575 (1997).
    • (1997) Acta Crystallogr. A , vol.53 , pp. 564-575
    • Ursby, T.1    Bourgeois, D.2
  • 29
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software system for macromolecular structure determination
    • Brünger, A. T. et al. Crystallography and NMR system: A new software system for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 31
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R. M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. 15, 133-138 (1997).
    • (1997) J. Mol. Graph. , vol.15 , pp. 133-138
    • Esnouf, R.M.1
  • 32
    • 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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