Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP Analog

The structure of the ternary complex consisting of yeast phenylalanyl-transfer RNA (Phe-tRNA Phe ), Thermus aquaticus elongation factor Tu (EF-Tu), and the guanosine triphosphate (GTP) analog GDPNP was determined by x-ray crystallography at 2.7 angstrom resolution. The ternary complex participates i...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1995-12, Vol.270 (5241), p.1464-1472
Main Authors: Nissen, Poul, Kjeldgaard, Morten, Thirup, Søren, Polekhina, Galina, Reshetnikova, Ludmila, Clark, Brian F. C., Nyborg, Jens
Format: Article
Language:English
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c984-e8b020d4a61def4cb152632fcb6d699e47ee0597a5aefb213e245fb774339f293
cites cdi_FETCH-LOGICAL-c984-e8b020d4a61def4cb152632fcb6d699e47ee0597a5aefb213e245fb774339f293
container_end_page 1472
container_issue 5241
container_start_page 1464
container_title Science (American Association for the Advancement of Science)
container_volume 270
creator Nissen, Poul
Kjeldgaard, Morten
Thirup, Søren
Polekhina, Galina
Reshetnikova, Ludmila
Clark, Brian F. C.
Nyborg, Jens
description The structure of the ternary complex consisting of yeast phenylalanyl-transfer RNA (Phe-tRNA Phe ), Thermus aquaticus elongation factor Tu (EF-Tu), and the guanosine triphosphate (GTP) analog GDPNP was determined by x-ray crystallography at 2.7 angstrom resolution. The ternary complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome. The EF-Tu-GDPNP component binds to one side of the acceptor helix of Phe-tRNA Phe involving all three domains of EF-Tu. Binding sites for the phenylalanylated CCA end and the phosphorylated 5′ end are located at domain interfaces, whereas the T stem interacts with the surface of the β-barrel domain 3. The binding involves many conserved residues in EF-Tu. The overall shape of the ternary complex is similar to that of the translocation factor, EF-G-GDP, and this suggests a novel mechanism involving "molecular mimicry" in the translational apparatus.
doi_str_mv 10.1126/science.270.5241.1464
format article
fullrecord <record><control><sourceid>crossref</sourceid><recordid>TN_cdi_crossref_primary_10_1126_science_270_5241_1464</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>10_1126_science_270_5241_1464</sourcerecordid><originalsourceid>FETCH-LOGICAL-c984-e8b020d4a61def4cb152632fcb6d699e47ee0597a5aefb213e245fb774339f293</originalsourceid><addsrcrecordid>eNot0F1LwzAUBuAgCs7pTxDyA5aa7y6Xo-xDGDpm70OanrhJ146kBffvXXFX5-UcOLw8CL0ymjHG9VvyR2g9ZDynmeKSZUxqeYcmjBpFDKfiHk0oFZrMaa4e0VNKP5Reb0ZM0L6Il9S7Bn_1cfD9EAF3AfcHwCXE1sULLrrTuYHfcb07AOn3H4sx4Blerkg5zLBra-zwutzhReua7vsZPQTXJHi5zSkqV8uy2JDt5_q9WGyJN3NJYF5RTmvpNKshSF8xxbXgwVe61saAzAGoMrlTDkLFmQAuVajyXAphAjdiitT_Wx-7lCIEe47H07WxZdSOLvbmYq8udnSxo4v4A52yVlQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP Analog</title><source>American Association for the Advancement of Science</source><source>Social Science Premium Collection</source><source>Education Collection</source><creator>Nissen, Poul ; Kjeldgaard, Morten ; Thirup, Søren ; Polekhina, Galina ; Reshetnikova, Ludmila ; Clark, Brian F. C. ; Nyborg, Jens</creator><creatorcontrib>Nissen, Poul ; Kjeldgaard, Morten ; Thirup, Søren ; Polekhina, Galina ; Reshetnikova, Ludmila ; Clark, Brian F. C. ; Nyborg, Jens</creatorcontrib><description>The structure of the ternary complex consisting of yeast phenylalanyl-transfer RNA (Phe-tRNA Phe ), Thermus aquaticus elongation factor Tu (EF-Tu), and the guanosine triphosphate (GTP) analog GDPNP was determined by x-ray crystallography at 2.7 angstrom resolution. The ternary complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome. The EF-Tu-GDPNP component binds to one side of the acceptor helix of Phe-tRNA Phe involving all three domains of EF-Tu. Binding sites for the phenylalanylated CCA end and the phosphorylated 5′ end are located at domain interfaces, whereas the T stem interacts with the surface of the β-barrel domain 3. The binding involves many conserved residues in EF-Tu. The overall shape of the ternary complex is similar to that of the translocation factor, EF-G-GDP, and this suggests a novel mechanism involving "molecular mimicry" in the translational apparatus.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.270.5241.1464</identifier><language>eng</language><ispartof>Science (American Association for the Advancement of Science), 1995-12, Vol.270 (5241), p.1464-1472</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c984-e8b020d4a61def4cb152632fcb6d699e47ee0597a5aefb213e245fb774339f293</citedby><cites>FETCH-LOGICAL-c984-e8b020d4a61def4cb152632fcb6d699e47ee0597a5aefb213e245fb774339f293</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2882,2883,27923,27924</link.rule.ids></links><search><creatorcontrib>Nissen, Poul</creatorcontrib><creatorcontrib>Kjeldgaard, Morten</creatorcontrib><creatorcontrib>Thirup, Søren</creatorcontrib><creatorcontrib>Polekhina, Galina</creatorcontrib><creatorcontrib>Reshetnikova, Ludmila</creatorcontrib><creatorcontrib>Clark, Brian F. C.</creatorcontrib><creatorcontrib>Nyborg, Jens</creatorcontrib><title>Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP Analog</title><title>Science (American Association for the Advancement of Science)</title><description>The structure of the ternary complex consisting of yeast phenylalanyl-transfer RNA (Phe-tRNA Phe ), Thermus aquaticus elongation factor Tu (EF-Tu), and the guanosine triphosphate (GTP) analog GDPNP was determined by x-ray crystallography at 2.7 angstrom resolution. The ternary complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome. The EF-Tu-GDPNP component binds to one side of the acceptor helix of Phe-tRNA Phe involving all three domains of EF-Tu. Binding sites for the phenylalanylated CCA end and the phosphorylated 5′ end are located at domain interfaces, whereas the T stem interacts with the surface of the β-barrel domain 3. The binding involves many conserved residues in EF-Tu. The overall shape of the ternary complex is similar to that of the translocation factor, EF-G-GDP, and this suggests a novel mechanism involving "molecular mimicry" in the translational apparatus.</description><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNot0F1LwzAUBuAgCs7pTxDyA5aa7y6Xo-xDGDpm70OanrhJ146kBffvXXFX5-UcOLw8CL0ymjHG9VvyR2g9ZDynmeKSZUxqeYcmjBpFDKfiHk0oFZrMaa4e0VNKP5Reb0ZM0L6Il9S7Bn_1cfD9EAF3AfcHwCXE1sULLrrTuYHfcb07AOn3H4sx4Blerkg5zLBra-zwutzhReua7vsZPQTXJHi5zSkqV8uy2JDt5_q9WGyJN3NJYF5RTmvpNKshSF8xxbXgwVe61saAzAGoMrlTDkLFmQAuVajyXAphAjdiitT_Wx-7lCIEe47H07WxZdSOLvbmYq8udnSxo4v4A52yVlQ</recordid><startdate>199512</startdate><enddate>199512</enddate><creator>Nissen, Poul</creator><creator>Kjeldgaard, Morten</creator><creator>Thirup, Søren</creator><creator>Polekhina, Galina</creator><creator>Reshetnikova, Ludmila</creator><creator>Clark, Brian F. C.</creator><creator>Nyborg, Jens</creator><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>199512</creationdate><title>Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP Analog</title><author>Nissen, Poul ; Kjeldgaard, Morten ; Thirup, Søren ; Polekhina, Galina ; Reshetnikova, Ludmila ; Clark, Brian F. C. ; Nyborg, Jens</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c984-e8b020d4a61def4cb152632fcb6d699e47ee0597a5aefb213e245fb774339f293</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nissen, Poul</creatorcontrib><creatorcontrib>Kjeldgaard, Morten</creatorcontrib><creatorcontrib>Thirup, Søren</creatorcontrib><creatorcontrib>Polekhina, Galina</creatorcontrib><creatorcontrib>Reshetnikova, Ludmila</creatorcontrib><creatorcontrib>Clark, Brian F. C.</creatorcontrib><creatorcontrib>Nyborg, Jens</creatorcontrib><collection>CrossRef</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nissen, Poul</au><au>Kjeldgaard, Morten</au><au>Thirup, Søren</au><au>Polekhina, Galina</au><au>Reshetnikova, Ludmila</au><au>Clark, Brian F. C.</au><au>Nyborg, Jens</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP Analog</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><date>1995-12</date><risdate>1995</risdate><volume>270</volume><issue>5241</issue><spage>1464</spage><epage>1472</epage><pages>1464-1472</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><abstract>The structure of the ternary complex consisting of yeast phenylalanyl-transfer RNA (Phe-tRNA Phe ), Thermus aquaticus elongation factor Tu (EF-Tu), and the guanosine triphosphate (GTP) analog GDPNP was determined by x-ray crystallography at 2.7 angstrom resolution. The ternary complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome. The EF-Tu-GDPNP component binds to one side of the acceptor helix of Phe-tRNA Phe involving all three domains of EF-Tu. Binding sites for the phenylalanylated CCA end and the phosphorylated 5′ end are located at domain interfaces, whereas the T stem interacts with the surface of the β-barrel domain 3. The binding involves many conserved residues in EF-Tu. The overall shape of the ternary complex is similar to that of the translocation factor, EF-G-GDP, and this suggests a novel mechanism involving "molecular mimicry" in the translational apparatus.</abstract><doi>10.1126/science.270.5241.1464</doi><tpages>9</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0036-8075
ispartof Science (American Association for the Advancement of Science), 1995-12, Vol.270 (5241), p.1464-1472
issn 0036-8075
1095-9203
language eng
recordid cdi_crossref_primary_10_1126_science_270_5241_1464
source American Association for the Advancement of Science; Social Science Premium Collection; Education Collection
title Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP Analog
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-12T02%3A06%3A18IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-crossref&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Crystal%20Structure%20of%20the%20Ternary%20Complex%20of%20Phe-tRNA%20Phe%20,%20EF-Tu,%20and%20a%20GTP%20Analog&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Nissen,%20Poul&rft.date=1995-12&rft.volume=270&rft.issue=5241&rft.spage=1464&rft.epage=1472&rft.pages=1464-1472&rft.issn=0036-8075&rft.eissn=1095-9203&rft_id=info:doi/10.1126/science.270.5241.1464&rft_dat=%3Ccrossref%3E10_1126_science_270_5241_1464%3C/crossref%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c984-e8b020d4a61def4cb152632fcb6d699e47ee0597a5aefb213e245fb774339f293%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true