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| | ==IF2-G2 GDP complex== | | ==IF2-G2 GDP complex== |
| - | <StructureSection load='2lkd' size='340' side='right' caption='[[2lkd]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | + | <StructureSection load='2lkd' size='340' side='right'caption='[[2lkd]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lkd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LKD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lkd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LKD 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">Solution NMR</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lkc|2lkc]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">infB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</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=2lkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkd OCA], [https://pdbe.org/2lkd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lkd RCSB], [https://www.ebi.ac.uk/pdbsum/2lkd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lkd ProSAT]</span></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=2lkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkd OCA], [http://pdbe.org/2lkd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lkd RCSB], [http://www.ebi.ac.uk/pdbsum/2lkd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lkd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IF2_GEOSE IF2_GEOSE]] 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. | + | [https://www.uniprot.org/uniprot/IF2_GEOSE IF2_GEOSE] 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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 12980]] | + | [[Category: Geobacillus stearothermophilus]] |
| - | [[Category: Belardinelli, R]] | + | [[Category: Large Structures]] |
| - | [[Category: Boelens, R]] | + | [[Category: Belardinelli R]] |
| - | [[Category: Dongre, R]] | + | [[Category: Boelens R]] |
| - | [[Category: Folkers, G E]] | + | [[Category: Dongre R]] |
| - | [[Category: Gualerzi, C O]] | + | [[Category: Folkers GE]] |
| - | [[Category: Spurio, R]] | + | [[Category: Gualerzi CO]] |
| - | [[Category: Tishchenko, E]] | + | [[Category: Spurio R]] |
| - | [[Category: Tomaselli, S]] | + | [[Category: Tishchenko E]] |
| - | [[Category: Wienk, H]] | + | [[Category: Tomaselli S]] |
| - | [[Category: Translation]]
| + | [[Category: Wienk H]] |
| Structural highlights
Function
IF2_GEOSE 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.
Publication Abstract from PubMed
Bacterial translation initiation factor IF2 promotes ribosomal subunit association, recruitment, and binding of fMet-tRNA to the ribosomal P-site and initiation dipeptide formation. Here, we present the solution structures of GDP-bound and apo-IF2-G2 of Bacillus stearothermophilus and provide evidence that this isolated domain binds the 50 S ribosomal subunit and hydrolyzes GTP. Differences between the free and GDP-bound structures of IF2-G2 suggest that domain reorganization within the G2-G3-C1 regions underlies the different structural requirements of IF2 during the initiation process. However, these structural signals are unlikely forwarded from IF2-G2 to the C-terminal fMet-tRNA binding domain (IF2-C2) because the connected IF2-C1 and IF2-C2 modules show completely independent mobility, indicating that the bacterial interdomain connector lacks the rigidity that was found in the archaeal IF2 homolog aIF5B.
Structural Dynamics of Bacterial Translation Initiation Factor IF2.,Wienk H, Tishchenko E, Belardinelli R, Tomaselli S, Dongre R, Spurio R, Folkers GE, Gualerzi CO, Boelens R J Biol Chem. 2012 Mar 30;287(14):10922-32. Epub 2012 Feb 3. PMID:22308033[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wienk H, Tishchenko E, Belardinelli R, Tomaselli S, Dongre R, Spurio R, Folkers GE, Gualerzi CO, Boelens R. Structural Dynamics of Bacterial Translation Initiation Factor IF2. J Biol Chem. 2012 Mar 30;287(14):10922-32. Epub 2012 Feb 3. PMID:22308033 doi:10.1074/jbc.M111.333393
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