structure of LepA, the ribosomal back translocase
LepA is a highly conserved elongation factor that promotes the back translocation of tRNAs on the ribosome during the elongation cycle. We have determined the crystal structure of LepA from Escherichia coli at 2.8-Å resolution. The high degree of sequence identity between LepA and EF-G is reflected...
Gespeichert in:
| Veröffentlicht in: | Proc. Natl. Acad. Sci. USA 2008-03, Vol.105 (12), p.4673-4678 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 4678 |
|---|---|
| container_issue | 12 |
| container_start_page | 4673 |
| container_title | Proc. Natl. Acad. Sci. USA |
| container_volume | 105 |
| creator | Evans, Robin N Blaha, Gregor Bailey, Scott Steitz, Thomas A |
| description | LepA is a highly conserved elongation factor that promotes the back translocation of tRNAs on the ribosome during the elongation cycle. We have determined the crystal structure of LepA from Escherichia coli at 2.8-Å resolution. The high degree of sequence identity between LepA and EF-G is reflected in the structural similarity between the individual homologous domains of LepA and EF-G. However, the orientation of domains III and V in LepA differs from their orientations in EF-G. LepA also contains a C-terminal domain (CTD) not found in EF-G that has a previously unobserved protein fold. The high structural similarity between LepA and EF-G enabled us to derive a homology model for LepA bound to the ribosome using a 7.3-Å cryo-EM structure of a complex between EF-G and the 70S ribosome. In this model, the very electrostatically positive CTD of LepA is placed in the direct vicinity of the A site of the large ribosomal subunit, suggesting a possible interaction between the CTD and the back translocated tRNA or 23S rRNA. |
| doi_str_mv | 10.1073/pnas.0801308105 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2290774</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>25461481</jstor_id><sourcerecordid>25461481</sourcerecordid><originalsourceid>FETCH-LOGICAL-c552t-1b64f7b7e28f30a168cea60860ad07d560fd90bb654522e5fdcd0f2e43aecea3</originalsourceid><addsrcrecordid>eNqF0Utv1DAUBWALgei0sGYFRCwQC9JeO35lg1RVvKSRWFDWluNcd1Iy8WA7CP59Hc2oAxtYeeHPx_fqEPKMwjkF1VzsJpvOQQNtQFMQD8iKQktryVt4SFYATNWaM35CTlO6BYBWaHhMTqhuJGsatiI05Ti7PEesgq_WuLt8W-UNVnHoQgpbO1addd-rHO2UxuBswifkkbdjwqeH84xcf3h_ffWpXn_5-Pnqcl07IViuaSe5V51Cpn0Dlkrt0ErQEmwPqhcSfN9C10nBBWMofO968Ax5Y7HI5oy828fu5m6LvcOpzDCaXRy2Nv42wQ7m75tp2Jib8NMw1oJSvAS82geElAeT3JDRbVyYJnTZUAApqSjo9eGXGH7MmLLZDsnhONoJw5yMAs4ka_l_IQPdgmhpgRd76GJIKaK_H5mCWTozS2fm2Fl58eLPTY_-UFIBbw5geXmME4Yyw2WJ9PM4ZvyVC335b1rE8724TTnEe8IEl5RrekzwNhh7E4dkvn1ly7CglV4WuAMJHb0o</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>20890591</pqid></control><display><type>article</type><title>structure of LepA, the ribosomal back translocase</title><source>MEDLINE</source><source>JSTOR Archive Collection A-Z Listing</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Evans, Robin N ; Blaha, Gregor ; Bailey, Scott ; Steitz, Thomas A</creator><creatorcontrib>Evans, Robin N ; Blaha, Gregor ; Bailey, Scott ; Steitz, Thomas A ; Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><description>LepA is a highly conserved elongation factor that promotes the back translocation of tRNAs on the ribosome during the elongation cycle. We have determined the crystal structure of LepA from Escherichia coli at 2.8-Å resolution. The high degree of sequence identity between LepA and EF-G is reflected in the structural similarity between the individual homologous domains of LepA and EF-G. However, the orientation of domains III and V in LepA differs from their orientations in EF-G. LepA also contains a C-terminal domain (CTD) not found in EF-G that has a previously unobserved protein fold. The high structural similarity between LepA and EF-G enabled us to derive a homology model for LepA bound to the ribosome using a 7.3-Å cryo-EM structure of a complex between EF-G and the 70S ribosome. In this model, the very electrostatically positive CTD of LepA is placed in the direct vicinity of the A site of the large ribosomal subunit, suggesting a possible interaction between the CTD and the back translocated tRNA or 23S rRNA.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0801308105</identifier><identifier>PMID: 18362332</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Bacteria ; Binding Sites ; Biological Sciences ; Charge transfer devices ; Crystal structure ; Crystallography, X-Ray ; Crystals ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli Proteins - chemistry ; Hydrolysis ; Lepas ; Models, Molecular ; Nucleotides ; Nucleotides - metabolism ; Peptide Elongation Factor G - chemistry ; Peptide elongation factors ; Peptide Initiation Factors ; Peptidyl Transferases - chemistry ; Protein Binding ; Protein Structure, Tertiary ; Ribosomes ; Ribosomes - enzymology ; RNA, Transfer - metabolism ; Structural Homology, Protein ; Transcriptional Elongation Factors - chemistry ; Transfer RNA</subject><ispartof>Proc. Natl. Acad. Sci. USA, 2008-03, Vol.105 (12), p.4673-4678</ispartof><rights>Copyright 2008 The National Academy of Sciences of the United States of America</rights><rights>2008 by The National Academy of Sciences of the USA</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c552t-1b64f7b7e28f30a168cea60860ad07d560fd90bb654522e5fdcd0f2e43aecea3</citedby><cites>FETCH-LOGICAL-c552t-1b64f7b7e28f30a168cea60860ad07d560fd90bb654522e5fdcd0f2e43aecea3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/105/12.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/25461481$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/25461481$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,728,781,785,804,886,27928,27929,53795,53797,58021,58254</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18362332$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1006615$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Evans, Robin N</creatorcontrib><creatorcontrib>Blaha, Gregor</creatorcontrib><creatorcontrib>Bailey, Scott</creatorcontrib><creatorcontrib>Steitz, Thomas A</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>structure of LepA, the ribosomal back translocase</title><title>Proc. Natl. Acad. Sci. USA</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>LepA is a highly conserved elongation factor that promotes the back translocation of tRNAs on the ribosome during the elongation cycle. We have determined the crystal structure of LepA from Escherichia coli at 2.8-Å resolution. The high degree of sequence identity between LepA and EF-G is reflected in the structural similarity between the individual homologous domains of LepA and EF-G. However, the orientation of domains III and V in LepA differs from their orientations in EF-G. LepA also contains a C-terminal domain (CTD) not found in EF-G that has a previously unobserved protein fold. The high structural similarity between LepA and EF-G enabled us to derive a homology model for LepA bound to the ribosome using a 7.3-Å cryo-EM structure of a complex between EF-G and the 70S ribosome. In this model, the very electrostatically positive CTD of LepA is placed in the direct vicinity of the A site of the large ribosomal subunit, suggesting a possible interaction between the CTD and the back translocated tRNA or 23S rRNA.</description><subject>Bacteria</subject><subject>Binding Sites</subject><subject>Biological Sciences</subject><subject>Charge transfer devices</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Crystals</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Hydrolysis</subject><subject>Lepas</subject><subject>Models, Molecular</subject><subject>Nucleotides</subject><subject>Nucleotides - metabolism</subject><subject>Peptide Elongation Factor G - chemistry</subject><subject>Peptide elongation factors</subject><subject>Peptide Initiation Factors</subject><subject>Peptidyl Transferases - chemistry</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Ribosomes</subject><subject>Ribosomes - enzymology</subject><subject>RNA, Transfer - metabolism</subject><subject>Structural Homology, Protein</subject><subject>Transcriptional Elongation Factors - chemistry</subject><subject>Transfer RNA</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0Utv1DAUBWALgei0sGYFRCwQC9JeO35lg1RVvKSRWFDWluNcd1Iy8WA7CP59Hc2oAxtYeeHPx_fqEPKMwjkF1VzsJpvOQQNtQFMQD8iKQktryVt4SFYATNWaM35CTlO6BYBWaHhMTqhuJGsatiI05Ti7PEesgq_WuLt8W-UNVnHoQgpbO1addd-rHO2UxuBswifkkbdjwqeH84xcf3h_ffWpXn_5-Pnqcl07IViuaSe5V51Cpn0Dlkrt0ErQEmwPqhcSfN9C10nBBWMofO968Ax5Y7HI5oy828fu5m6LvcOpzDCaXRy2Nv42wQ7m75tp2Jib8NMw1oJSvAS82geElAeT3JDRbVyYJnTZUAApqSjo9eGXGH7MmLLZDsnhONoJw5yMAs4ka_l_IQPdgmhpgRd76GJIKaK_H5mCWTozS2fm2Fl58eLPTY_-UFIBbw5geXmME4Yyw2WJ9PM4ZvyVC335b1rE8724TTnEe8IEl5RrekzwNhh7E4dkvn1ly7CglV4WuAMJHb0o</recordid><startdate>20080325</startdate><enddate>20080325</enddate><creator>Evans, Robin N</creator><creator>Blaha, Gregor</creator><creator>Bailey, Scott</creator><creator>Steitz, Thomas A</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</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>7QL</scope><scope>7TM</scope><scope>C1K</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>20080325</creationdate><title>structure of LepA, the ribosomal back translocase</title><author>Evans, Robin N ; Blaha, Gregor ; Bailey, Scott ; Steitz, Thomas A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c552t-1b64f7b7e28f30a168cea60860ad07d560fd90bb654522e5fdcd0f2e43aecea3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Bacteria</topic><topic>Binding Sites</topic><topic>Biological Sciences</topic><topic>Charge transfer devices</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Crystals</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Hydrolysis</topic><topic>Lepas</topic><topic>Models, Molecular</topic><topic>Nucleotides</topic><topic>Nucleotides - metabolism</topic><topic>Peptide Elongation Factor G - chemistry</topic><topic>Peptide elongation factors</topic><topic>Peptide Initiation Factors</topic><topic>Peptidyl Transferases - chemistry</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Ribosomes</topic><topic>Ribosomes - enzymology</topic><topic>RNA, Transfer - metabolism</topic><topic>Structural Homology, Protein</topic><topic>Transcriptional Elongation Factors - chemistry</topic><topic>Transfer RNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Evans, Robin N</creatorcontrib><creatorcontrib>Blaha, Gregor</creatorcontrib><creatorcontrib>Bailey, Scott</creatorcontrib><creatorcontrib>Steitz, Thomas A</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proc. Natl. Acad. Sci. USA</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Evans, Robin N</au><au>Blaha, Gregor</au><au>Bailey, Scott</au><au>Steitz, Thomas A</au><aucorp>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>structure of LepA, the ribosomal back translocase</atitle><jtitle>Proc. Natl. Acad. Sci. USA</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2008-03-25</date><risdate>2008</risdate><volume>105</volume><issue>12</issue><spage>4673</spage><epage>4678</epage><pages>4673-4678</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>LepA is a highly conserved elongation factor that promotes the back translocation of tRNAs on the ribosome during the elongation cycle. We have determined the crystal structure of LepA from Escherichia coli at 2.8-Å resolution. The high degree of sequence identity between LepA and EF-G is reflected in the structural similarity between the individual homologous domains of LepA and EF-G. However, the orientation of domains III and V in LepA differs from their orientations in EF-G. LepA also contains a C-terminal domain (CTD) not found in EF-G that has a previously unobserved protein fold. The high structural similarity between LepA and EF-G enabled us to derive a homology model for LepA bound to the ribosome using a 7.3-Å cryo-EM structure of a complex between EF-G and the 70S ribosome. In this model, the very electrostatically positive CTD of LepA is placed in the direct vicinity of the A site of the large ribosomal subunit, suggesting a possible interaction between the CTD and the back translocated tRNA or 23S rRNA.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>18362332</pmid><doi>10.1073/pnas.0801308105</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proc. Natl. Acad. Sci. USA, 2008-03, Vol.105 (12), p.4673-4678 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2290774 |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Bacteria Binding Sites Biological Sciences Charge transfer devices Crystal structure Crystallography, X-Ray Crystals Escherichia coli Escherichia coli - enzymology Escherichia coli Proteins - chemistry Hydrolysis Lepas Models, Molecular Nucleotides Nucleotides - metabolism Peptide Elongation Factor G - chemistry Peptide elongation factors Peptide Initiation Factors Peptidyl Transferases - chemistry Protein Binding Protein Structure, Tertiary Ribosomes Ribosomes - enzymology RNA, Transfer - metabolism Structural Homology, Protein Transcriptional Elongation Factors - chemistry Transfer RNA |
| title | structure of LepA, the ribosomal back translocase |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-16T20%3A04%3A12IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=structure%20of%20LepA,%20the%20ribosomal%20back%20translocase&rft.jtitle=Proc.%20Natl.%20Acad.%20Sci.%20USA&rft.au=Evans,%20Robin%20N&rft.aucorp=Argonne%20National%20Lab.%20(ANL),%20Argonne,%20IL%20(United%20States).%20Advanced%20Photon%20Source%20(APS)&rft.date=2008-03-25&rft.volume=105&rft.issue=12&rft.spage=4673&rft.epage=4678&rft.pages=4673-4678&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.0801308105&rft_dat=%3Cjstor_pubme%3E25461481%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=20890591&rft_id=info:pmid/18362332&rft_jstor_id=25461481&rfr_iscdi=true |