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| | ==Crystal Structure of Thermus Thermophilus IF2, Apo and GDP-bound Forms (2-474)== | | ==Crystal Structure of Thermus Thermophilus IF2, Apo and GDP-bound Forms (2-474)== |
| - | <StructureSection load='4kjz' size='340' side='right' caption='[[4kjz]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='4kjz' size='340' side='right'caption='[[4kjz]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kjz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus_hb8 Thermus thermophilus hb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KJZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KJZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kjz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KJZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">infB, TTHA0699 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 Thermus thermophilus HB8])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4kjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kjz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kjz RCSB], [http://www.ebi.ac.uk/pdbsum/4kjz PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4kjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kjz OCA], [https://pdbe.org/4kjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kjz RCSB], [https://www.ebi.ac.uk/pdbsum/4kjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kjz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IF2_THET8 IF2_THET8]] One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity). | + | [https://www.uniprot.org/uniprot/IF2_THET8 IF2_THET8] One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4kjz" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Thermus thermophilus hb8]] | + | [[Category: Large Structures]] |
| - | [[Category: Eiler, D R]] | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Lin, J]] | + | [[Category: Eiler DR]] |
| - | [[Category: Steitz, T A]] | + | [[Category: Lin J]] |
| - | [[Category: Gtp]] | + | [[Category: Steitz TA]] |
| - | [[Category: Gtpase]]
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| - | [[Category: Translation]]
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| - | [[Category: Translation initiation factor/if2 superfamily]]
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| Structural highlights
Function
IF2_THET8 One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity).
Publication Abstract from PubMed
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-A 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.
Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases.,Eiler D, Lin J, Simonetti A, Klaholz BP, Steitz TA Proc Natl Acad Sci U S A. 2013 Sep 24;110(39):15662-7. doi:, 10.1073/pnas.1309360110. Epub 2013 Sep 12. PMID:24029018[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Eiler D, Lin J, Simonetti A, Klaholz BP, Steitz TA. Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases. Proc Natl Acad Sci U S A. 2013 Sep 24;110(39):15662-7. doi:, 10.1073/pnas.1309360110. Epub 2013 Sep 12. PMID:24029018 doi:10.1073/pnas.1309360110
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