How a G Protein Binds a Membrane
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 prote...
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| Veröffentlicht in: | The Journal of biological chemistry 2004-08, Vol.279 (32), p.33937-33945 |
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| container_end_page | 33945 |
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| container_issue | 32 |
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| container_title | The Journal of biological chemistry |
| container_volume | 279 |
| creator | Zhang, Zhixian Melia, Thomas J. He, Feng Yuan, Ching McGough, Amy Schmid, Michael F. Wensel, Theodore G. |
| description | 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. |
| doi_str_mv | 10.1074/jbc.M403404200 |
| format | Article |
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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. 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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.</description><subject>Animals</subject><subject>Binding Sites</subject><subject>Cattle</subject><subject>Cell Membrane - metabolism</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>Ice</subject><subject>Image Processing, Computer-Assisted</subject><subject>Lipid Bilayers - chemistry</subject><subject>Lipid Bilayers - metabolism</subject><subject>Membrane Lipids - chemistry</subject><subject>Membrane Lipids - metabolism</subject><subject>Microscopy, Electron</subject><subject>Models, Molecular</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - metabolism</subject><subject>Protein Binding</subject><subject>Protein Structure, Secondary</subject><subject>Rod Cell Outer Segment - chemistry</subject><subject>Transducin - chemistry</subject><subject>Transducin - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1LAzEQhoMotlavHmUP4m1rvjabHLVoK7ToQcFbyCazNqXbrcnW4r83sgVPzmVgeN6X4UHokuAxwSW_XVV2vOCYccwpxkdoSLBkOSvI-zEaYkxJrmghB-gsxhVOwxU5RQNSkJIRyYcom7X7zGTT7CW0HfhNdu83LqbLApoqmA2co5ParCNcHPYIvT0-vE5m-fx5-jS5m-eWY9XlRDiGTSVr4kgNXDFZOyGq0oKg1DBrCsorSUtBmFFGYsOpUbSWVIKzhAEboZu-dxvazx3ETjc-Wliv0w_tLmohSlEIThI47kEb2hgD1HobfGPCtyZY_zrRyYn-c5ICV4fmXdWA-8MPEhJw3QNL_7Hc-wC68q1dQqNpqTSjmjHFyoTJHoOk4ctD0NF62FhwKWI77Vr_3ws_ycR4Yw</recordid><startdate>20040806</startdate><enddate>20040806</enddate><creator>Zhang, Zhixian</creator><creator>Melia, Thomas J.</creator><creator>He, Feng</creator><creator>Yuan, Ching</creator><creator>McGough, Amy</creator><creator>Schmid, Michael F.</creator><creator>Wensel, Theodore G.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20040806</creationdate><title>How a G Protein Binds a Membrane</title><author>Zhang, Zhixian ; Melia, Thomas J. ; He, Feng ; Yuan, Ching ; McGough, Amy ; Schmid, Michael F. ; Wensel, Theodore G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-16d30ab8f1d1fe4938fd66b7ce622a3ca524b827613a9a80a42a92f828edc13e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Binding Sites</topic><topic>Cattle</topic><topic>Cell Membrane - metabolism</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>Ice</topic><topic>Image Processing, Computer-Assisted</topic><topic>Lipid Bilayers - chemistry</topic><topic>Lipid Bilayers - metabolism</topic><topic>Membrane Lipids - chemistry</topic><topic>Membrane Lipids - metabolism</topic><topic>Microscopy, Electron</topic><topic>Models, Molecular</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - metabolism</topic><topic>Protein Binding</topic><topic>Protein Structure, Secondary</topic><topic>Rod Cell Outer Segment - chemistry</topic><topic>Transducin - chemistry</topic><topic>Transducin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Zhixian</creatorcontrib><creatorcontrib>Melia, Thomas J.</creatorcontrib><creatorcontrib>He, Feng</creatorcontrib><creatorcontrib>Yuan, Ching</creatorcontrib><creatorcontrib>McGough, Amy</creatorcontrib><creatorcontrib>Schmid, Michael F.</creatorcontrib><creatorcontrib>Wensel, Theodore G.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Zhixian</au><au>Melia, Thomas J.</au><au>He, Feng</au><au>Yuan, Ching</au><au>McGough, Amy</au><au>Schmid, Michael F.</au><au>Wensel, Theodore G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>How a G Protein Binds a Membrane</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-08-06</date><risdate>2004</risdate><volume>279</volume><issue>32</issue><spage>33937</spage><epage>33945</epage><pages>33937-33945</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><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. 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| ispartof | The Journal of biological chemistry, 2004-08, Vol.279 (32), p.33937-33945 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Binding Sites Cattle Cell Membrane - metabolism Crystallization Crystallography, X-Ray Ice Image Processing, Computer-Assisted Lipid Bilayers - chemistry Lipid Bilayers - metabolism Membrane Lipids - chemistry Membrane Lipids - metabolism Microscopy, Electron Models, Molecular Peptide Fragments - chemistry Peptide Fragments - metabolism Protein Binding Protein Structure, Secondary Rod Cell Outer Segment - chemistry Transducin - chemistry Transducin - metabolism |
| title | How a G Protein Binds a Membrane |
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