Visualization of elongation factor Tu on the Escherichia coli ribosome
The delivery of a specific amino acid to the translating ribosome is fundamental to protein synthesis. The binding of aminoacyl-transfer RNA to the ribosome is catalysed by the elongation factor Tu (EF-Tu). The elongation factor, the aminoacyl-tRNA and GTP form a stable 'ternary' complex t...
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| Veröffentlicht in: | Nature (London) 1997-09, Vol.389 (6649), p.403-406 |
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| creator | Heel, Marin van Stark, Holger Rodnina, Marina V Rinke-Appel, Jutta Brimacombe, Richard Wintermeyer, Wolfgang |
| description | The delivery of a specific amino acid to the translating ribosome is fundamental to protein synthesis. The binding of aminoacyl-transfer RNA to the ribosome is catalysed by the elongation factor Tu (EF-Tu). The elongation factor, the aminoacyl-tRNA and GTP form a stable 'ternary' complex that binds to the ribosome. We have used electron cryomicroscopy and angular reconstitution to visualize directly the kirromycin-stalled ternary complex in the A site of the 70S ribosome of Escherichia coli. Electron cryomicroscopy had previously given detailed ribosomal structures at 25 and 23 Å (refs 2, 3) resolution, and was used to determine the position of tRNAs on the ribosome. In particular, the structures of pre-translocational (tRNAs in A and P sites) and post-translocational ribosomes (P and E sites occupied) were both visualized at a resolution of ∼20 Å. Our three-dimensional reconstruction at 18 Å resolution shows the ternary complex spanning the inter-subunit space with the acceptor domain of the tRNA reaching into the decoding centre. Domain 1 (the G domain) of the EF-Tu is bound both to the L7/L12 stalk and to the 50S body underneath the stalk, whereas domain 2 is oriented towards the S12 region on the 30S subunit. |
| doi_str_mv | 10.1038/38770 |
| format | Article |
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The binding of aminoacyl-transfer RNA to the ribosome is catalysed by the elongation factor Tu (EF-Tu). The elongation factor, the aminoacyl-tRNA and GTP form a stable 'ternary' complex that binds to the ribosome. We have used electron cryomicroscopy and angular reconstitution to visualize directly the kirromycin-stalled ternary complex in the A site of the 70S ribosome of Escherichia coli. Electron cryomicroscopy had previously given detailed ribosomal structures at 25 and 23 Å (refs 2, 3) resolution, and was used to determine the position of tRNAs on the ribosome. In particular, the structures of pre-translocational (tRNAs in A and P sites) and post-translocational ribosomes (P and E sites occupied) were both visualized at a resolution of ∼20 Å. Our three-dimensional reconstruction at 18 Å resolution shows the ternary complex spanning the inter-subunit space with the acceptor domain of the tRNA reaching into the decoding centre. Domain 1 (the G domain) of the EF-Tu is bound both to the L7/L12 stalk and to the 50S body underneath the stalk, whereas domain 2 is oriented towards the S12 region on the 30S subunit.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/38770</identifier><identifier>PMID: 9311785</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino acids ; Bacteria ; Bacteriology ; Biological and medical sciences ; Crystallography, X-Ray ; E coli ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Fundamental and applied biological sciences. Psychology ; Genetics ; Guanosine Triphosphate - chemistry ; Guanosine Triphosphate - metabolism ; Humanities and Social Sciences ; letter ; Microbiology ; Models, Molecular ; multidisciplinary ; Nucleic Acid Conformation ; Peptide Elongation Factor Tu - chemistry ; Peptide Elongation Factor Tu - drug effects ; Peptide Elongation Factor Tu - metabolism ; Peptide Elongation Factor Tu - ultrastructure ; Protein Conformation ; Protein synthesis ; Pyridones - pharmacology ; Ribosomes - chemistry ; Ribosomes - drug effects ; Ribosomes - metabolism ; Ribosomes - ultrastructure ; RNA, Transfer - metabolism ; Science ; Science (multidisciplinary) ; Scientific imaging</subject><ispartof>Nature (London), 1997-09, Vol.389 (6649), p.403-406</ispartof><rights>Macmillan Magazines Ltd. 1997</rights><rights>1997 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. 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The binding of aminoacyl-transfer RNA to the ribosome is catalysed by the elongation factor Tu (EF-Tu). The elongation factor, the aminoacyl-tRNA and GTP form a stable 'ternary' complex that binds to the ribosome. We have used electron cryomicroscopy and angular reconstitution to visualize directly the kirromycin-stalled ternary complex in the A site of the 70S ribosome of Escherichia coli. Electron cryomicroscopy had previously given detailed ribosomal structures at 25 and 23 Å (refs 2, 3) resolution, and was used to determine the position of tRNAs on the ribosome. In particular, the structures of pre-translocational (tRNAs in A and P sites) and post-translocational ribosomes (P and E sites occupied) were both visualized at a resolution of ∼20 Å. Our three-dimensional reconstruction at 18 Å resolution shows the ternary complex spanning the inter-subunit space with the acceptor domain of the tRNA reaching into the decoding centre. 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Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Heel, Marin van</au><au>Stark, Holger</au><au>Rodnina, Marina V</au><au>Rinke-Appel, Jutta</au><au>Brimacombe, Richard</au><au>Wintermeyer, Wolfgang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Visualization of elongation factor Tu on the Escherichia coli ribosome</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1997-09-25</date><risdate>1997</risdate><volume>389</volume><issue>6649</issue><spage>403</spage><epage>406</epage><pages>403-406</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>The delivery of a specific amino acid to the translating ribosome is fundamental to protein synthesis. The binding of aminoacyl-transfer RNA to the ribosome is catalysed by the elongation factor Tu (EF-Tu). The elongation factor, the aminoacyl-tRNA and GTP form a stable 'ternary' complex that binds to the ribosome. We have used electron cryomicroscopy and angular reconstitution to visualize directly the kirromycin-stalled ternary complex in the A site of the 70S ribosome of Escherichia coli. Electron cryomicroscopy had previously given detailed ribosomal structures at 25 and 23 Å (refs 2, 3) resolution, and was used to determine the position of tRNAs on the ribosome. In particular, the structures of pre-translocational (tRNAs in A and P sites) and post-translocational ribosomes (P and E sites occupied) were both visualized at a resolution of ∼20 Å. Our three-dimensional reconstruction at 18 Å resolution shows the ternary complex spanning the inter-subunit space with the acceptor domain of the tRNA reaching into the decoding centre. Domain 1 (the G domain) of the EF-Tu is bound both to the L7/L12 stalk and to the 50S body underneath the stalk, whereas domain 2 is oriented towards the S12 region on the 30S subunit.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>9311785</pmid><doi>10.1038/38770</doi><tpages>4</tpages></addata></record> |
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| ispartof | Nature (London), 1997-09, Vol.389 (6649), p.403-406 |
| issn | 0028-0836 1476-4687 |
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| subjects | Amino acids Bacteria Bacteriology Biological and medical sciences Crystallography, X-Ray E coli Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Fundamental and applied biological sciences. Psychology Genetics Guanosine Triphosphate - chemistry Guanosine Triphosphate - metabolism Humanities and Social Sciences letter Microbiology Models, Molecular multidisciplinary Nucleic Acid Conformation Peptide Elongation Factor Tu - chemistry Peptide Elongation Factor Tu - drug effects Peptide Elongation Factor Tu - metabolism Peptide Elongation Factor Tu - ultrastructure Protein Conformation Protein synthesis Pyridones - pharmacology Ribosomes - chemistry Ribosomes - drug effects Ribosomes - metabolism Ribosomes - ultrastructure RNA, Transfer - metabolism Science Science (multidisciplinary) Scientific imaging |
| title | Visualization of elongation factor Tu on the Escherichia coli ribosome |
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