Abstract
RECENT evidence shows that membrane-bound proteins can be crystallized successfully in the presence of detergent1-3, which seems to facilitate the ordered packing of the proteins by binding to their hydrophobic surfaces in micellar manner4,5. This approach has enabled the molecular structures of two bacterial photosynthetic reaction centres to be solved at high resolution by X-ray crystallography6-9, each of which has provided insights into the mechanism of photo-activated electron transport across the cell membrane. The detergent, however, although present in high concentration in the crystals, is not seen in these high-resolution structures because of disordering. To determine the structural motifs formed by the detergent that are involved in crystal packing, we have therefore generated a low-resolution structure using neutron diffraction with contrast variation. We find that the detergent is concentrated in rings which fill all the available space around the membrane-spanning α-helices of the reaction-centre protein subunits L, M and H. These rings are interconnected throughout the crystal lattice by short cylindrical detergent bridges such that zig-zag chains are formed parallel to the c direction. The average structure of the detergent therefore is spatially complementary to the structure of the reaction-centre complex and provides a model for the interaction between the lipid bilayer and the complex in vivo.
Similar content being viewed by others
References
Michel, H. & Oesterhelt, D. Proc. natn. Acad. Sci. U.S.A. 77, 1283–1285 (1980).
Garavito, M. & Rosenbusch, J. P. J. Cell Biol. 86, 327–329 (1980).
Michel, H. J. molec. Biol. 158, 567–572 (1982).
Michel, H. Trends biochem. Sci. 8, 56–59 (1983).
Garavito, R. M., Markovic-Housley, Z. & Jenkins, J. A. J. Crystal Growth 76, 701–709 (1986).
Deisenhofer, J., Epp, O., Miki, K., Huber, R. & Michel, H. J. molec. Biol. 180, 385–398 (1984).
Deisenhofer, J., Epp, O., Miki, K., Huber, R. & Michel, H. Nature 318, 618–624 (1985).
Allen, J. P., Feher, G., Yeates, T. O., Komiya, H. & Rees, D. C. Proc. natn. Acad. Sci. U.S.A. 84, 5730–5734 (1987).
Allen, J. P., Feher, G., Yeates, T. O., Komiya, H. & Rees, D. C. Proc. natn. Acad. Sci. U.S.A. 84, 6162–6166 (1987).
Bentley, G. A., Lewit-Bentley, A., Finch, J. T., Podjarny, A. D. & Roth, M. J. molec. Biol. 176, 55–75 (1984).
Roth, M., Lewit-Bentley, A. & Bentley, G. A. J. appl. Crystallogr. 17, 77–84 (1984).
Roth, M. Acta crystallogr. A43, 780–787 (1987).
Sardet, C., Tardieu, A. & Luzzatti, V. J. molec. Biol. 105, 383–407 (1976).
Lewis, B. & Engelman, D. J. molec. Biol. 166, 211–217 (1983).
Yeates, T. O., Komiya, H., Rees, D. C., Allen, J. P. & Feher, G. Proc. natn. Acad. Sci. U.S.A. 84, 6438–6442 (1987).
Jay, F., Lambilotte, M., Stark, W. & Mühlethaler, K. EMBO J. 4, 773–776 (1984).
Stark, W., Kühlbrandt, W., Wildhaber, I., Wehrli, E. & Müthlethaler, K. EMBO J. 4, 777–783 (1984).
Allemand, R., Bourdel, J., Roudaut, E., Convert, P., Ibel, K., Jacobe, J., Cotton, J. P. & Farnoux, B. Nucl. Instrum. Meth. 126, 29–42 (1975).
Roche, C. T., Strauss, M. G. & Brenner, R. IEEE Trans. Nucl. Sci. NS-32, 373–379 (1985).
Roth, M. & Lewit-Bentley, A. in Journal de Physique 47, Colloque C5, Workshop on Software for Evaluation of Data from PSD (ed. Mclntyre, G. J.) C5 27–C5 34 (1986).
Roth, M. & Lewit-Bentley, A. Acta crystallogr. A38, 670–679 (1982).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Roth, M., Lewit-Bentley, A., Michel, H. et al. Detergent structure in crystals of a bacterial photosynthetic reaction centre. Nature 340, 659–662 (1989). https://doi.org/10.1038/340659a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/340659a0
- Springer Nature Limited
This article is cited by
-
Quantification of Detergents Complexed with Membrane Proteins
Scientific Reports (2017)
-
Signalling under the microscope
Nature (2017)
-
Semiquinone oscillations as a tool for investigating the ubiquinone binding to photosynthetic reaction centers
European Biophysics Journal (2015)
-
A review of factors affecting the success of membrane protein crystallization using bicelles
Frontiers in Biology (2013)