Conformational change of helix G in the bacteriorhodopsin photocycle: Investigation with heavy atom labeling and x-ray diffraction

Biophysical Journal

Volumn 76, Issue 2, 1999, Pages 1018-1023

  Oka, Toshihiko ^a   Kamikubo, Hironari ^a,e   Tokunaga, Fumio ^a   Lanyi, Janos K ^b   Needleman, Richard ^c   Kataoka, Mikio ^a,d  

^a OSAKA UNIVERSITY   (Japan)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^e INSTITUTE OF MATERIALS STRUCTURE SCIENCE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; MERCURY;

ANALYTICAL EQUIPMENT; ARTICLE; CHEMICAL LABELING; CONFORMATIONAL TRANSITION; FOURIER ANALYSIS; HALOBACTERIUM SALINARUM; NONHUMAN; PROTEIN CONFORMATION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; X RAY DIFFRACTION;

EID: 0033059345     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77266-8     Document Type: Article

References (30)

1. Amemiya, Y., K. Wakabayashi, T. Hamanaka, T. Wakabayashi, T. Matsushita, and H. Hashizume. 1983. Design of a small-angle x-ray diffractometer using synchrotron radiation at the photon factory. Nucl. Instrum. Methods. 208:471-477.
2. Dencher, N. A., D. Dresselhaus, G. Zaccai, and G. Büldt. 1989. Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction. Proc. Natl. Acad. Sci. USA. 86:7876-7879.
3. Grigorieff, N., T. A. Ceska, K. H. Downing, J. M. Baldwin, and R. Henderson. 1996. Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 259:393-421.
4. Hauss, T., G. Büldt, M. P. Heyn, and N. A. Dencher. 1994. Light-induced isomerization causes chromophore tilts in the M intermediate of bacteriorhodopsin: a neutron diffraction study. Proc. Natl. Acad. Sci. USA. 91:11854-11858.
5. Henderson, R., J. Baldwin, T. A. Ceska, F. Zemlin, E. Beckmann, and K. H. Downing. 1990. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213: 899-929.
6. Kamikubo, H., M. Kataoka, G. Váró, T. Oka, F. Tokunaga, R. Needleman, and J. K. Lanyi. 1996. Structure of the N intermediate of bacteriorhodopsin revealed by x-ray diffraction. Proc. Natl. Acad. Sci. USA. 93: 1386-1390.
7. Kamikubo, H., T. Oka, Y. Imamoto, F. Tokunaga, J. K. Lanyi, and M. Kataoka. 1997. 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: 12282-12287.
8. Kataoka, M., H. Kamikubo, F. Tokunaga, L. S. Brown, Y. Yamazaki, A. Maeda, M. Sheves, R. Needleman, and J. K. Lanyi. 1994. Energy coupling in an ion pump. The reprotonation switch of bacteriorhodopsin. J. Mol. Biol. 243:621-638.
9. Kimura, Y., D. G. Vassylyev, A. Miyazawa, A. Kidera, M. Matsushima, K. Mitsuoka, K. Murata, T. Hirai, and Y. Fujiyoshi. 1997. Surface of bacteriorhodopsin revealed by high-resolution electron crystallography. Nature. 389:206-211.
10. Koch, M. H., N. A. Dencher, D. Oesterhelt, H.-J. Plöhn, G. Rapp, and G. Büldt. 1991. Time-resolved x-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin. EMBO J. 10: 521-526.
11. Krebs, M. P., W. Behrens, R. Mollaaghababa, H. G. Khorana, and M. P. Heyn. 1993. X-ray diffraction of a cysteine-containing bacteriorhodopsin mutant and its mercury derivative. Localization of an amino acid residue in the loop of an integral membrane protein. Biochemistry. 32:12830-12834.
12. Lanyi, J. K. 1995. Bacteriorhodopsin as a model for proton pumps. Nature. 375:461-463.
13. Lanyi, J. K. 1997. Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps. J. Biol. Chem. 272: 31209-31212.
14. Ludlam, C. F. C., S. Sonar, C.-P. Lee, M. Coleman, J. Herzfeld, U. L. Rajbhandary, and K. J. Rothschild. 1995. Site-directed isotope labeling and ATR-FTIR difference spectroscopy of bacteriorhodopsin: the peptide carbonyl group of Tyr 185 is structurally active during the bR→N transition. Biochemistry. 34:2-6.
15. Luecke, H., H. T. Richter, and J. K. Lanyi. 1998. Proton transfer pathway in bacteriorhodopsin at 2.3 Angstrom resolution. Science. 280:1934-37.
16. Nakasako, M., M. Kataoka, Y. Amemiya, and F. Tokunaga. 1991. Crystallographic characterization by x-ray diffraction of the M-intermediate from the photo-cycle of bacteriorhodopsin at room temperature. FEBS Lett. 292:73-75.
17. 85 both participate in a counterion and proton acceptor complex near the Schiff base. J. Biol. Chem. 266:11478-11484.
18. Ni, B., M. Chang, A. Duschl, J. K. Lanyi, and R. Needleman. 1990. An efficient system for the synthesis of bacteriorhodopsin in Halobacterium halobium. Gene. 90:169-172.
19. Oesterhelt, D., and W. Stoeckenius. 1974. Isolation of cell membrane of Halobcterium halobium and its fractionation into red and purple membrane. Methods Enzymol. 31:667-678.
20. Oka, T., H. Kamikubo, F. Tokunaga, J. K. Lanyi, R. Needleman, and M. Kataoka. 1997. X-ray diffraction studies of bacteriorhodopsin. Determines of the positions of mercury label at several engineered cysteine residues. Photochem. Photobiol. 66:768-773.
21. Pebay-Peyroula, E., G. Rummel, J. P. Rosenbusch, E. M. Landau. 1997. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science. 277:1676-1681.
22. Pfefferlé, J. M., A. Maeda, J. Sasaki, and T. Yoshizawa. 1991. Fourier transform infrared study of the N intermediate of bacteriorhodopsin. Biochemistry. 30:6548-6556.
23. Plöhn, H.-J., and G. Büldt. 1989. The determination of label positions in membrane proteins by neutron and anomalous x-ray diffraction of powder samples. J. Appl. Crystallogr. 19:255-261.
24. 96 → Asn bacteriorhodopsin. J. Biol. Chem. 267:20782-20786.
25. Sass, H. J., I. W. Schachowa, G. Rapp, M. H. J. Koch, D. Oesterhelt, N. A. Dencher, and G. Büldt. 1997. The tertiary structural changes in bacteriorhodopsin occur between M states: x-ray diffraction and Fourier transform infrared spectroscopy. EMBO J. 16:1484-1491.
26. Subramaniam, S., M. Gerstein, D. Oesterhelt, and R. Henderson. 1993. Electron diffraction analysis of structural change in the photocycle of bacteriorhodopsin. EMBO J. 12:1-8.
27. Takei, H., Y. Gat, Z. Rothman, A. Lewis, and M. Sheves. 1994. Active site lysine backbone undergoes conformational changes in the bacteriorhodopsin photocycle. J. Biol. Chem. 269:7387-7389.
28. Thorgesirsson, T. E., W. Xiao, L. S. Brown, R. Needleman, J. K. Lanyi, and Y.-K. Shin. 1997. Transient channel-oepning in bacteriorhodopsin: an EPR study. J. Mol. Biol. 273:951-957.
29. Váró, G., and J. K. Lanyi. 1991. Thermodynamics and energy coupling in the bacteriorhodopsin photocycle. Biochemistry. 30:5008-5015.
30. Vonck, J. 1996. 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.