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Originally published In Press as doi:10.1074/jbc.M403404200 on June 1, 2004

J. Biol. Chem., Vol. 279, Issue 32, 33937-33945, August 6, 2004
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How a G Protein Binds a Membrane*

Zhixian Zhang, Thomas J. Melia{ddagger}, Feng He, Ching Yuan§, Amy McGough, Michael F. Schmid, and Theodore G. Wensel||

From the Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030

Heterotrimeric G proteins interact with receptors and effectors at the membrane-cytoplasm interface. Structures of soluble forms have not revealed how they interact with membranes. We have used electron crystallography to determine the structure in ice of a helical array of the photoreceptor G protein, transducin, bound to the surface of a tubular lipid bilayer. The protein binds to the membrane with a very small area of contact, restricted to two points, between the surface of the protein and the surface of the lipids. Fitting the x-ray structure into the membrane-bound structure reveals one membrane contact near the lipidated G{gamma} C terminus and G{alpha} N terminus, and another near the G{alpha} C terminus. The narrowness of the tethers to the lipid bilayer provides flexibility for the protein to adopt multiple orientations on the membrane, and leaves most of the G protein surface area available for protein-protein interactions.

Received for publication, March 26, 2004 , and in revised form, May 26, 2004.

* This work was supported in part by National Institutes of Health Grant EY07981, National Center for Macromolecular Imaging Grant RR02250, and the Welch Foundation. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{ddagger} Supported by Houston Area Molecular Biophysics Program Grant T32-GM08280. Present address: Memorial Sloan-Kettering Cancer Center, New York, NY 10021.

§ Present address: Dept. of Ophthalmology, University of Minnesota Medical School, Minneapolis, MN 55455.

Present address: Dept. of Biological Sciences, Purdue University, West Lafayette, IN 47907-1392.

|| To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030. Tel.: 713-798-6994; Fax: 713-796-9438; E-mail: twensel{at}bcm.tmc.edu.


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