The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution
Elongation factor G (EF‐G) catalyzes the translocation step of protein synthesis in bacteria, and like the other bacterial elongation factor, EF‐Tu‐‐whose structure is already known‐‐it is a member of the GTPase superfamily. We have determined the crystal structure of EF‐G‐‐GDP from Thermus thermoph...
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| Veröffentlicht in: | The EMBO journal 1994-08, Vol.13 (16), p.3661-3668 |
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| creator | Czworkowski, J. Wang, J. Steitz, T.A. Moore, P.B. |
| description | Elongation factor G (EF‐G) catalyzes the translocation step of protein synthesis in bacteria, and like the other bacterial elongation factor, EF‐Tu‐‐whose structure is already known‐‐it is a member of the GTPase superfamily. We have determined the crystal structure of EF‐G‐‐GDP from Thermus thermophilus. It is an elongated molecule whose large, N‐terminal domain resembles the G domain of EF‐Tu, except for a 90 residue insert, which covers a surface that is involved in nucleotide exchange in EF‐Tu and other G proteins. The tertiary structures of the second domains of EF‐G and EF‐Tu are nearly identical, but the relative placement of the first two domains in EF‐G‐‐GDP resembles that seen in EF‐Tu‐‐GTP, not EF‐Tu‐‐GDP. The remaining three domains of EF‐G look like RNA binding domains, and have no counterparts in EF‐Tu. |
| doi_str_mv | 10.1002/j.1460-2075.1994.tb06675.x |
| format | Article |
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We have determined the crystal structure of EF‐G‐‐GDP from Thermus thermophilus. It is an elongated molecule whose large, N‐terminal domain resembles the G domain of EF‐Tu, except for a 90 residue insert, which covers a surface that is involved in nucleotide exchange in EF‐Tu and other G proteins. The tertiary structures of the second domains of EF‐G and EF‐Tu are nearly identical, but the relative placement of the first two domains in EF‐G‐‐GDP resembles that seen in EF‐Tu‐‐GTP, not EF‐Tu‐‐GDP. The remaining three domains of EF‐G look like RNA binding domains, and have no counterparts in EF‐Tu.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1002/j.1460-2075.1994.tb06675.x</identifier><identifier>PMID: 8070396</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; GTP Phosphohydrolase-Linked Elongation Factors - chemistry ; GTP Phosphohydrolase-Linked Elongation Factors - metabolism ; Guanosine Diphosphate - chemistry ; Models, Molecular ; Molecular Sequence Data ; Peptide Chain Elongation, Translational ; Peptide Elongation Factor G ; Peptide Elongation Factor Tu - chemistry ; Peptide Elongation Factors - chemistry ; Peptide Elongation Factors - metabolism ; Thermus thermophilus - chemistry ; Thermus thermophilus - enzymology</subject><ispartof>The EMBO journal, 1994-08, Vol.13 (16), p.3661-3668</ispartof><rights>1994 European Molecular Biology Organization</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3935-24e29fef2c9139c3821d9ff261a330b9f3368e7785001ae0f8cdcfa5df3be6203</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC395276/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC395276/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8070396$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Czworkowski, J.</creatorcontrib><creatorcontrib>Wang, J.</creatorcontrib><creatorcontrib>Steitz, T.A.</creatorcontrib><creatorcontrib>Moore, P.B.</creatorcontrib><title>The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><description>Elongation factor G (EF‐G) catalyzes the translocation step of protein synthesis in bacteria, and like the other bacterial elongation factor, EF‐Tu‐‐whose structure is already known‐‐it is a member of the GTPase superfamily. We have determined the crystal structure of EF‐G‐‐GDP from Thermus thermophilus. It is an elongated molecule whose large, N‐terminal domain resembles the G domain of EF‐Tu, except for a 90 residue insert, which covers a surface that is involved in nucleotide exchange in EF‐Tu and other G proteins. The tertiary structures of the second domains of EF‐G and EF‐Tu are nearly identical, but the relative placement of the first two domains in EF‐G‐‐GDP resembles that seen in EF‐Tu‐‐GTP, not EF‐Tu‐‐GDP. The remaining three domains of EF‐G look like RNA binding domains, and have no counterparts in EF‐Tu.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Crystallography, X-Ray</subject><subject>GTP Phosphohydrolase-Linked Elongation Factors - chemistry</subject><subject>GTP Phosphohydrolase-Linked Elongation Factors - metabolism</subject><subject>Guanosine Diphosphate - chemistry</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Peptide Chain Elongation, Translational</subject><subject>Peptide Elongation Factor G</subject><subject>Peptide Elongation Factor Tu - chemistry</subject><subject>Peptide Elongation Factors - chemistry</subject><subject>Peptide Elongation Factors - metabolism</subject><subject>Thermus thermophilus - chemistry</subject><subject>Thermus thermophilus - enzymology</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkc1uEzEUhS0EKiHwCEgWC1bM9NrO_BiJRSglpSqCRVhbjue6mcgZp7aHJm_PDIkiWHZlW8ffvUfnEPKOQc4A-OUmZ7MSMg5VkTMpZ3laQVkOj_0zMjlLz8kEeMmyGavlS_Iqxg0AFHXFLshFDRUIWU7IcrlGasIhJu1oTKE3qQ9IvaXofHevU-s7arVJPtAFNX67c7jHhj62aU0XX35-oDpRnld0TgNG7_oReE1eWO0ivjmdU_Lr6_Xy6ia7-7H4djW_y4yQosj4DLm0aLmRTEgjas4aae3gWQsBK2mFKGusqroAYBrB1qYxVheNFSssOYgp-XScu-tXW2wMdilop3ah3epwUF636n-la9fq3v9WQha8Kgf-_YkP_qHHmNS2jQad0x36PqpqDJUN5qbk4_GjCT7GgPa8g4EaK1EbNeauxtzVWIk6VaL2A_z2X5dn9NTBoM-P-mPr8PCEyer6--fbv3fxB9y_nWY</recordid><startdate>19940815</startdate><enddate>19940815</enddate><creator>Czworkowski, J.</creator><creator>Wang, J.</creator><creator>Steitz, T.A.</creator><creator>Moore, P.B.</creator><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><scope>5PM</scope></search><sort><creationdate>19940815</creationdate><title>The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution</title><author>Czworkowski, J. ; Wang, J. ; Steitz, T.A. ; Moore, P.B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3935-24e29fef2c9139c3821d9ff261a330b9f3368e7785001ae0f8cdcfa5df3be6203</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Crystallography, X-Ray</topic><topic>GTP Phosphohydrolase-Linked Elongation Factors - chemistry</topic><topic>GTP Phosphohydrolase-Linked Elongation Factors - metabolism</topic><topic>Guanosine Diphosphate - chemistry</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Peptide Chain Elongation, Translational</topic><topic>Peptide Elongation Factor G</topic><topic>Peptide Elongation Factor Tu - chemistry</topic><topic>Peptide Elongation Factors - chemistry</topic><topic>Peptide Elongation Factors - metabolism</topic><topic>Thermus thermophilus - chemistry</topic><topic>Thermus thermophilus - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Czworkowski, J.</creatorcontrib><creatorcontrib>Wang, J.</creatorcontrib><creatorcontrib>Steitz, T.A.</creatorcontrib><creatorcontrib>Moore, P.B.</creatorcontrib><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Czworkowski, J.</au><au>Wang, J.</au><au>Steitz, T.A.</au><au>Moore, P.B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1994-08-15</date><risdate>1994</risdate><volume>13</volume><issue>16</issue><spage>3661</spage><epage>3668</epage><pages>3661-3668</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><abstract>Elongation factor G (EF‐G) catalyzes the translocation step of protein synthesis in bacteria, and like the other bacterial elongation factor, EF‐Tu‐‐whose structure is already known‐‐it is a member of the GTPase superfamily. We have determined the crystal structure of EF‐G‐‐GDP from Thermus thermophilus. It is an elongated molecule whose large, N‐terminal domain resembles the G domain of EF‐Tu, except for a 90 residue insert, which covers a surface that is involved in nucleotide exchange in EF‐Tu and other G proteins. The tertiary structures of the second domains of EF‐G and EF‐Tu are nearly identical, but the relative placement of the first two domains in EF‐G‐‐GDP resembles that seen in EF‐Tu‐‐GTP, not EF‐Tu‐‐GDP. The remaining three domains of EF‐G look like RNA binding domains, and have no counterparts in EF‐Tu.</abstract><cop>England</cop><pmid>8070396</pmid><doi>10.1002/j.1460-2075.1994.tb06675.x</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0261-4189 |
| ispartof | The EMBO journal, 1994-08, Vol.13 (16), p.3661-3668 |
| issn | 0261-4189 1460-2075 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Binding Sites Crystallography, X-Ray GTP Phosphohydrolase-Linked Elongation Factors - chemistry GTP Phosphohydrolase-Linked Elongation Factors - metabolism Guanosine Diphosphate - chemistry Models, Molecular Molecular Sequence Data Peptide Chain Elongation, Translational Peptide Elongation Factor G Peptide Elongation Factor Tu - chemistry Peptide Elongation Factors - chemistry Peptide Elongation Factors - metabolism Thermus thermophilus - chemistry Thermus thermophilus - enzymology |
| title | The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution |
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