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1z9b
From Proteopedia
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(New page: 200px<br /><applet load="1z9b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z9b" /> '''Solution structure of the C1-subdomain of Ba...) |
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| - | [[Image:1z9b.gif|left|200px]]<br /><applet load="1z9b" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1z9b" /> | ||
| - | '''Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2'''<br /> | ||
| - | == | + | ==Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2== |
| - | IF2 is one of three bacterial translation initiation factors that are | + | <StructureSection load='1z9b' size='340' side='right'caption='[[1z9b]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1z9b]] 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=1Z9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z9B FirstGlance]. <br> | ||
| + | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z9b OCA], [https://pdbe.org/1z9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z9b RCSB], [https://www.ebi.ac.uk/pdbsum/1z9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z9b ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z9/1z9b_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1z9b ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | IF2 is one of three bacterial translation initiation factors that are conserved through all kingdoms of life. It binds the 30S and 50S ribosomal subunits, as well as fMet-tRNAf(Met). After these interactions, fMet-tRNAf(Met) is oriented to the ribosomal P-site where the first amino acid of the nascent polypeptide, formylmethionine, is presented. The C-terminal domain of Bacillus stearothermophilus IF2, which is responsible for recognition and binding of fMet-tRNAf(Met), contains two structured modules. Previously, the solution structure of the most C-terminal module, IF2-C2, has been elucidated by NMR spectroscopy and direct interactions between this subdomain and fMet-tRNAf(Met) were reported. In the present NMR study we have obtained the spectral assignment of the other module of the C-terminal domain (IF2-C1) and determined its solution structure and backbone dynamics. The IF2-C1 core forms a flattened fold consisting of a central four-stranded parallel beta-sheet flanked by three alpha-helices. Although its overall organization resembles that of subdomain III of the archaeal IF2-homolog eIF5B whose crystal structure had previously been reported, some differences of potential functional significance are evident. | ||
| - | + | Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2.,Wienk H, Tomaselli S, Bernard C, Spurio R, Picone D, Gualerzi CO, Boelens R Protein Sci. 2005 Sep;14(9):2461-8. Epub 2005 Aug 4. PMID:16081655<ref>PMID:16081655</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1z9b" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Bernard | + | [[Category: Bernard C]] |
| - | [[Category: Boelens | + | [[Category: Boelens R]] |
| - | [[Category: Gualerzi | + | [[Category: Gualerzi CO]] |
| - | [[Category: Picone | + | [[Category: Picone D]] |
| - | [[Category: Spurio | + | [[Category: Spurio R]] |
| - | [[Category: Tomaselli | + | [[Category: Tomaselli S]] |
| - | [[Category: Wienk | + | [[Category: Wienk H]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2
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