How a G protein binds a membrane

Zhixian Zhang, Thomas J. Melia, Feng He, Ching Yuan, Amy McGough, Michael F. Schmid, Theodore G. Wensel

Research output: Contribution to journalArticle

28 Scopus citations

Abstract

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 Gγ C terminus and Gα N terminus, and another near the Gα 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.

Original languageEnglish (US)
Pages (from-to)33937-33945
Number of pages9
JournalJournal of Biological Chemistry
Volume279
Issue number32
DOIs
StatePublished - Aug 6 2004

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    Zhang, Z., Melia, T. J., He, F., Yuan, C., McGough, A., Schmid, M. F., & Wensel, T. G. (2004). How a G protein binds a membrane. Journal of Biological Chemistry, 279(32), 33937-33945. https://doi.org/10.1074/jbc.M403404200