메뉴 건너뛰기




Volumn 1460, Issue 1, 2000, Pages 157-165

Crystallographic analysis of protein conformational changes in the bacteriorhodopsin photocycle

Author keywords

Electron microscopy; Time resolved crystallography

Indexed keywords

BACTERIORHODOPSIN; SCHIFF BASE;

EID: 0034734253     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(00)00136-5     Document Type: Review
Times cited : (42)

References (21)
  • 1
    • 0002979180 scopus 로고
    • Light energy transduction in bacteriorhodopsin
    • in: M. Jackson (Ed.), CRC Press, Boca Raton, FL
    • T.G. Ebrey, Light energy transduction in bacteriorhodopsin, in: M. Jackson (Ed.), Thermodynamics of Membrane Receptors and Channels, CRC Press, Boca Raton, FL, 1993, pp. 353-387.
    • (1993) Thermodynamics of Membrane Receptors and Channels , pp. 353-387
    • Ebrey, T.G.1
  • 2
    • 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
  • 3
    • 0025976082 scopus 로고
    • Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin
    • Koch M.H.J., Dencher N., Oesterhelt D., Plöhn H.-J., Rapp G., Büldt G. Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin. EMBO J. 10:1991;521-526.
    • (1991) EMBO J. , vol.10 , pp. 521-526
    • Koch, M.H.J.1    Dencher, N.2    Oesterhelt, D.3    Plöhn, H.-J.4    Rapp, G.5    Büldt, G.6
  • 4
    • 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., Amemiya Y., Tokunaga F. Crystallographic characterization by X-ray diffraction of the M intermediate from the photocycle of bacteriorhodopsin at room temperature. FEBS Lett. 292:1991;73-75.
    • (1991) FEBS Lett. , vol.292 , pp. 73-75
    • Nakasako, M.1    Kataoka, M.2    Amemiya, Y.3    Tokunaga, F.4
  • 6
    • 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
  • 7
    • 0028093220 scopus 로고
    • The bacteriorhodopsin photocycle: Direct structural study of two substates of the M-intermediate
    • Han B.-G., Vonck J., Glaeser R.M. The bacteriorhodopsin photocycle: direct structural study of two substates of the M-intermediate. Biophys. J. 67:1994;1179-1186.
    • (1994) Biophys. J. , vol.67 , pp. 1179-1186
    • Han, B.-G.1    Vonck, J.2    Glaeser, R.M.3
  • 8
    • 0029886089 scopus 로고    scopus 로고
    • A 3-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 3-dimensional difference map of the N-intermediate in the bacteriorhodopsin photocycle: part of the F-helix tilts in the M-to-N transition. Biochemistry. 35:1996;5870-5878.
    • (1996) Biochemistry , vol.35 , pp. 5870-5878
    • Vonck, J.1
  • 9
    • 0033548544 scopus 로고    scopus 로고
    • The projection structure of the low temperature K intermediate of the bacteriorhodopsin photocycle determined by electron diffraction
    • Bullough P., Henderson R. The projection structure of the low temperature K intermediate of the bacteriorhodopsin photocycle determined by electron diffraction. J. Mol. Biol. 286:1999;1663-1671.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1663-1671
    • Bullough, P.1    Henderson, R.2
  • 10
    • 0031684846 scopus 로고    scopus 로고
    • Structural characterization of the L-to-M transition of the bacteriorhodopsin photocycle
    • Hendrickson F.M., Burkard F., Glaeser R.M. Structural characterization of the L-to-M transition of the bacteriorhodopsin photocycle. Biophys. J. 75:1998;1446-1454.
    • (1998) Biophys. J. , vol.75 , pp. 1446-1454
    • Hendrickson, F.M.1    Burkard, F.2    Glaeser, R.M.3
  • 12
    • 0023024665 scopus 로고
    • Electron diffraction analysis of the M412 intermediate of bacteriorhodopsin
    • Glaeser R.M., Baldwin J.M., Ceska T.A., Henderson R. Electron diffraction analysis of the M412 intermediate of bacteriorhodopsin. Biophys. J. 50:1986;913-920.
    • (1986) Biophys. J. , vol.50 , pp. 913-920
    • Glaeser, R.M.1    Baldwin, J.M.2    Ceska, T.A.3    Henderson, R.4
  • 13
    • 0030901231 scopus 로고    scopus 로고
    • The tertiary structural changes in bacteriorhodopsin occur between M states: X-ray diffraction and Fourier transform infrared spectroscopy
    • Sass H.J., Schachowa I.W., Rapp G., Koch M.H.J., Oesterhelt D., Dencher N.A., Büldt G. The tertiary structural changes in bacteriorhodopsin occur between M states: X-ray diffraction and Fourier transform infrared spectroscopy. EMBO J. 16:1997;1484-1491.
    • (1997) EMBO J. , vol.16 , pp. 1484-1491
    • Sass, H.J.1    Schachowa, I.W.2    Rapp, G.3    Koch, M.H.J.4    Oesterhelt, D.5    Dencher, N.A.6    Büldt, G.7
  • 14
    • 0030813030 scopus 로고    scopus 로고
    • The last phase of the reprotonation switch in bacteriorhodopsin: The transition between the M-type and the N-type protein conformation depends on hydration
    • Kamikubo H., Oka T., Imamoto Y., Tokunaga F., Lanyi J.K., Kataoka M. The last phase of the reprotonation switch in bacteriorhodopsin: the transition between the M-type and the N-type protein conformation depends on hydration. Biochemistry. 36:1997;12282-12287.
    • (1997) Biochemistry , vol.36 , pp. 12282-12287
    • Kamikubo, H.1    Oka, T.2    Imamoto, Y.3    Tokunaga, F.4    Lanyi, J.K.5    Kataoka, M.6
  • 15
    • 0032579445 scopus 로고    scopus 로고
    • Structure and hydration of the M-state of the bacteriorhodopsin mutant D96N studied by neutron diffraction
    • Weik M., Zaccai G., Dencher N.A., Oesterhelt D. Structure and hydration of the M-state of the bacteriorhodopsin mutant D96N studied by neutron diffraction. J. Mol. Biol. 275:1998;625-634.
    • (1998) J. Mol. Biol. , vol.275 , pp. 625-634
    • Weik, M.1    Zaccai, G.2    Dencher, N.A.3    Oesterhelt, D.4
  • 16
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 Å resolution
    • Luecke H., Schobert B., Richter H.-T., Cartailler J.-P., Lanyi J.K. Structural changes in bacteriorhodopsin during ion transport at 2 Å resolution. Science. 286:1999;255-260.
    • (1999) Science , vol.286 , pp. 255-260
    • Luecke, H.1    Schobert, B.2    Richter, H.-T.3    Cartailler, J.-P.4    Lanyi, J.K.5
  • 19
    • 0028793135 scopus 로고
    • Molecular mechanism of protein-retinal coupling in bacteriorhodopsin
    • Delaney J.K., Schweiger U., Subramaniam S. Molecular mechanism of protein-retinal coupling in bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 92:1995;11120-11124.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11120-11124
    • Delaney, J.K.1    Schweiger, U.2    Subramaniam, S.3
  • 21
    • 0031042723 scopus 로고    scopus 로고
    • Electron diffraction studies of light-induced conformational changes in the Leu-93Ala bacteriorhodopsin mutant
    • Subramaniam S., Faruqi A.R., Oesterhelt D., Henderson R. Electron diffraction studies of light-induced conformational changes in the Leu-93Ala bacteriorhodopsin mutant. Proc. Natl. Acad. Sci. USA. 94:1997;1767-1772.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1767-1772
    • Subramaniam, S.1    Faruqi, A.R.2    Oesterhelt, D.3    Henderson, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.