Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases
The initiation of protein synthesis uses initiation factor 2 (IF2) in prokaryotes and a related protein named eukaryotic initiation factor 5B (eIF5B) in eukaryotes. IF2 is a GTPase that positions the initiator tRNA on the 30S ribosomal initiation complex and stimulates its assembly to the 50S riboso...
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| Veröffentlicht in: | Proc. Natl. Acad. Sci. USA 2013-09, Vol.110 (39), p.15662-15667 |
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| creator | Eiler, Daniel Lin, Jinzhong Simonetti, Angelita Klaholz, Bruno P. Steitz, Thomas A. |
| description | The initiation of protein synthesis uses initiation factor 2 (IF2) in prokaryotes and a related protein named eukaryotic initiation factor 5B (eIF5B) in eukaryotes. IF2 is a GTPase that positions the initiator tRNA on the 30S ribosomal initiation complex and stimulates its assembly to the 50S ribosomal subunit to make the 70S ribosome. The 3.1-Å resolution X-ray crystal structures of the full-length Thermus thermophilus apo IF2 and its complex with GDP presented here exhibit two different conformations (all of its domains except C2 domain are visible). Unlike all other translational GTPases, IF2 does not have an effecter domain that stably contacts the switch II region of the GTPase domain. The domain organization of IF2 is inconsistent with the “articulated lever” mechanism of communication between the GTPase and initiator tRNA binding domains that has been proposed for eIF5B. Previous cryo-electron microscopy reconstructions, NMR experiments, and this structure show that IF2 transitions from being flexible in solution to an extended conformation when interacting with ribosomal complexes. |
| doi_str_mv | 10.1073/pnas.1309360110 |
| format | Article |
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Previous cryo-electron microscopy reconstructions, NMR experiments, and this structure show that IF2 transitions from being flexible in solution to an extended conformation when interacting with ribosomal complexes.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1309360110</identifier><identifier>PMID: 24029018</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Binding sites ; Biochemical mechanisms ; Biochemistry, Molecular Biology ; Biological Sciences ; cryo-electron microscopy ; Crystal structure ; Crystallography, X-Ray ; Crystals ; Enzymes ; Eukaryotes ; eukaryotic cells ; Eukaryotic Initiation Factors - chemistry ; Eukaryotic Initiation Factors - metabolism ; GTP Phosphohydrolases - chemistry ; GTP Phosphohydrolases - metabolism ; guanosinetriphosphatase ; Hydrolysis ; Life Sciences ; Methanobacterium - metabolism ; Models, Molecular ; Molecular structure ; Molecules ; nuclear magnetic resonance spectroscopy ; Peptide initiation factors ; Prokaryotes ; prokaryotic cells ; Prokaryotic Initiation Factor-2 - chemistry ; Prokaryotic Initiation Factor-2 - metabolism ; Protein Biosynthesis ; Protein Structure, Secondary ; Protein Structure, Tertiary ; protein subunits ; Protein synthesis ; Proteins ; ribosomal proteins ; Ribosomes ; Thermus thermophilus ; Thermus thermophilus - metabolism ; Transfer RNA ; translation (genetics) ; X-ray diffraction</subject><ispartof>Proc. 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(ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases</title><title>Proc. Natl. Acad. Sci. USA</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The initiation of protein synthesis uses initiation factor 2 (IF2) in prokaryotes and a related protein named eukaryotic initiation factor 5B (eIF5B) in eukaryotes. IF2 is a GTPase that positions the initiator tRNA on the 30S ribosomal initiation complex and stimulates its assembly to the 50S ribosomal subunit to make the 70S ribosome. The 3.1-Å resolution X-ray crystal structures of the full-length Thermus thermophilus apo IF2 and its complex with GDP presented here exhibit two different conformations (all of its domains except C2 domain are visible). Unlike all other translational GTPases, IF2 does not have an effecter domain that stably contacts the switch II region of the GTPase domain. The domain organization of IF2 is inconsistent with the “articulated lever” mechanism of communication between the GTPase and initiator tRNA binding domains that has been proposed for eIF5B. Previous cryo-electron microscopy reconstructions, NMR experiments, and this structure show that IF2 transitions from being flexible in solution to an extended conformation when interacting with ribosomal complexes.</description><subject>Binding sites</subject><subject>Biochemical mechanisms</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological Sciences</subject><subject>cryo-electron microscopy</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Crystals</subject><subject>Enzymes</subject><subject>Eukaryotes</subject><subject>eukaryotic cells</subject><subject>Eukaryotic Initiation Factors - chemistry</subject><subject>Eukaryotic Initiation Factors - metabolism</subject><subject>GTP Phosphohydrolases - chemistry</subject><subject>GTP Phosphohydrolases - metabolism</subject><subject>guanosinetriphosphatase</subject><subject>Hydrolysis</subject><subject>Life Sciences</subject><subject>Methanobacterium - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular structure</subject><subject>Molecules</subject><subject>nuclear magnetic resonance spectroscopy</subject><subject>Peptide initiation factors</subject><subject>Prokaryotes</subject><subject>prokaryotic cells</subject><subject>Prokaryotic Initiation Factor-2 - chemistry</subject><subject>Prokaryotic Initiation Factor-2 - metabolism</subject><subject>Protein Biosynthesis</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>protein subunits</subject><subject>Protein synthesis</subject><subject>Proteins</subject><subject>ribosomal proteins</subject><subject>Ribosomes</subject><subject>Thermus thermophilus</subject><subject>Thermus thermophilus - metabolism</subject><subject>Transfer RNA</subject><subject>translation (genetics)</subject><subject>X-ray diffraction</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkkFv1DAQhSMEoqVw5gRYcIHDtuPYTuwLUqmgrVQJJNqzNes4uy4bu7WdSuW38GNxussC5cDJkv3Nm5nnV1XPKexTaNnBlce0Txko1gCl8KDapaDorOEKHla7AHU7k7zmO9WTlC4BQAkJj6udmkOtgMrd6sepd9lhdsGTHk0OkdTExNuUcUVSjqPJY7Qk2huLq0SQdK7vbbQ-ky4M6DwJcYHefd9IxDAQO37DeBuyM8T9oy4-EPQdGaxZlrI0EByCX5Ac0afVHVkaH59_wWTT0-pRX7raZ5tzr7r49PH86GR29vn49OjwbGaEbPKsF9jNeccESgXWADWm7hsuhQWLtUKUtmt6pTqJpsWmUzXOVcepamqQxTy2V71f616N88F2pmwXcaWvohvKIjqg03-_eLfUi3CjWStFy5oi8HotEFJ2OhmXy3omeG9N1uVHBBN1gd6toeU97ZPDMz3dAeeUAxM3tLBvNxPFcD3alPXgkrGrFXobxqSpBEYpbZj4P8pZS2nLOCvom3voZRhjMfyOklLRGibBgzVlYkgp2n47LAU9pU5PqdO_U1cqXv7p35b_FbMCkA0wVW7lih5Tmoqmmdx5sUYuU4nJluF1SxlTkyOv1u89Bo2L6JK--FoDbQAop6Is-BO-jfKn</recordid><startdate>20130924</startdate><enddate>20130924</enddate><creator>Eiler, Daniel</creator><creator>Lin, Jinzhong</creator><creator>Simonetti, Angelita</creator><creator>Klaholz, Bruno P.</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>1XC</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>20130924</creationdate><title>Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases</title><author>Eiler, Daniel ; 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Natl. Acad. Sci. USA</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Eiler, Daniel</au><au>Lin, Jinzhong</au><au>Simonetti, Angelita</au><au>Klaholz, Bruno P.</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>Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases</atitle><jtitle>Proc. Natl. Acad. Sci. USA</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2013-09-24</date><risdate>2013</risdate><volume>110</volume><issue>39</issue><spage>15662</spage><epage>15667</epage><pages>15662-15667</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The initiation of protein synthesis uses initiation factor 2 (IF2) in prokaryotes and a related protein named eukaryotic initiation factor 5B (eIF5B) in eukaryotes. IF2 is a GTPase that positions the initiator tRNA on the 30S ribosomal initiation complex and stimulates its assembly to the 50S ribosomal subunit to make the 70S ribosome. The 3.1-Å resolution X-ray crystal structures of the full-length Thermus thermophilus apo IF2 and its complex with GDP presented here exhibit two different conformations (all of its domains except C2 domain are visible). Unlike all other translational GTPases, IF2 does not have an effecter domain that stably contacts the switch II region of the GTPase domain. The domain organization of IF2 is inconsistent with the “articulated lever” mechanism of communication between the GTPase and initiator tRNA binding domains that has been proposed for eIF5B. Previous cryo-electron microscopy reconstructions, NMR experiments, and this structure show that IF2 transitions from being flexible in solution to an extended conformation when interacting with ribosomal complexes.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>24029018</pmid><doi>10.1073/pnas.1309360110</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Binding sites Biochemical mechanisms Biochemistry, Molecular Biology Biological Sciences cryo-electron microscopy Crystal structure Crystallography, X-Ray Crystals Enzymes Eukaryotes eukaryotic cells Eukaryotic Initiation Factors - chemistry Eukaryotic Initiation Factors - metabolism GTP Phosphohydrolases - chemistry GTP Phosphohydrolases - metabolism guanosinetriphosphatase Hydrolysis Life Sciences Methanobacterium - metabolism Models, Molecular Molecular structure Molecules nuclear magnetic resonance spectroscopy Peptide initiation factors Prokaryotes prokaryotic cells Prokaryotic Initiation Factor-2 - chemistry Prokaryotic Initiation Factor-2 - metabolism Protein Biosynthesis Protein Structure, Secondary Protein Structure, Tertiary protein subunits Protein synthesis Proteins ribosomal proteins Ribosomes Thermus thermophilus Thermus thermophilus - metabolism Transfer RNA translation (genetics) X-ray diffraction |
| title | Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases |
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