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How a G protein binds a membrane.

Zhixian Zhang·Thomas J Melia·Feng He·Ching Yuan·Amy McGough·Michael F Schmid·Theodore G Wensel
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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 Ggamma C terminus and Galpha N terminus, and another near the Galpha 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.

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AnimalsBinding SitesCattleCell MembraneCrystallizationCrystallography, X-RayIceImage Processing, Computer-AssistedLipid BilayersMembrane LipidsMicroscopy, ElectronModels, MolecularPeptide FragmentsProtein BindingProtein Structure, SecondaryRod Cell Outer SegmentTransducinJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.

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Zhixian Zhang, Thomas J Melia, Feng He, Ching Yuan, Amy McGough, Michael F Schmid, Theodore G Wensel. 2004-06-01. How a G protein binds a membrane.. https://doi.org/10.1074/jbc.m403404200

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