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==The structure of aIF2gamma subunit from the archaeon Sulfolobus solfataricus in the nucleotide-free form.== | |||
<StructureSection load='2plf' size='340' side='right'caption='[[2plf]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2plf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PLF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PLF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</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=2plf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2plf OCA], [https://pdbe.org/2plf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2plf RCSB], [https://www.ebi.ac.uk/pdbsum/2plf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2plf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/IF2G_SACS2 IF2G_SACS2] eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.[HAMAP-Rule:MF_00119] | |||
== 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/pl/2plf_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2plf ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Heterotrimeric a/eIF2alphabetagamma (archaeal homologue of the eukaryotic translation initiation factor 2 with alpha, beta and gamma subunits) delivers charged initiator tRNA (tRNAi) to the small ribosomal subunit. In this work, we determined the structures of aIF2gamma from the archaeon Sulfolobus solfataricus in the nucleotide-free and GDP-bound forms. Comparison of the free, GDP and Gpp(NH)p-Mg2+ forms of aIF2gamma revealed a sequence of conformational changes upon GDP and GTP binding. Our results show that the affinity of GDP to the G domain of the gamma subunit is higher than that of Gpp(NH)p. In analyzing a pyrophosphate molecule binding to domain II of the gamma subunit, we found a cleft that is very suitable for the acceptor stem of tRNA accommodation. It allows the suggestion of an alternative position for Met-tRNA i Met on the alphagamma intersubunit dimer, at variance with a recently published one. In the model reported here, the acceptor stem of the tRNAi is approximately perpendicular to that of tRNA in the ternary complex elongation factor Tu-Gpp(NH)p-tRNA. According to our analysis, the elbow and T stem of Met-tRNA i Met in this position should make extensive contact with the alpha subunit of aIF2. Thus, this model is in good agreement with experimental data showing that the alpha subunit of aIF2 is necessary for the stable interaction of aIF2gamma with Met-tRNA i Met. | |||
New insights into the interactions of the translation initiation factor 2 from archaea with guanine nucleotides and initiator tRNA.,Nikonov O, Stolboushkina E, Nikulin A, Hasenohrl D, Blasi U, Manstein DJ, Fedorov R, Garber M, Nikonov S J Mol Biol. 2007 Oct 19;373(2):328-36. Epub 2007 Aug 2. PMID:17825838<ref>PMID:17825838</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2plf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Blaesi | [[Category: Saccharolobus solfataricus]] | ||
[[Category: Fedorov | [[Category: Blaesi U]] | ||
[[Category: Garber | [[Category: Fedorov RV]] | ||
[[Category: Hasenohrl | [[Category: Garber MB]] | ||
[[Category: Manstein | [[Category: Hasenohrl D]] | ||
[[Category: Nikonov | [[Category: Manstein DJ]] | ||
[[Category: Nikonov | [[Category: Nikonov OS]] | ||
[[Category: Nikulin | [[Category: Nikonov SV]] | ||
[[Category: Stolboushkina | [[Category: Nikulin AD]] | ||
[[Category: Stolboushkina EA]] | |||
Latest revision as of 04:19, 21 November 2024
The structure of aIF2gamma subunit from the archaeon Sulfolobus solfataricus in the nucleotide-free form.The structure of aIF2gamma subunit from the archaeon Sulfolobus solfataricus in the nucleotide-free form.
Structural highlights
FunctionIF2G_SACS2 eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.[HAMAP-Rule:MF_00119] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHeterotrimeric a/eIF2alphabetagamma (archaeal homologue of the eukaryotic translation initiation factor 2 with alpha, beta and gamma subunits) delivers charged initiator tRNA (tRNAi) to the small ribosomal subunit. In this work, we determined the structures of aIF2gamma from the archaeon Sulfolobus solfataricus in the nucleotide-free and GDP-bound forms. Comparison of the free, GDP and Gpp(NH)p-Mg2+ forms of aIF2gamma revealed a sequence of conformational changes upon GDP and GTP binding. Our results show that the affinity of GDP to the G domain of the gamma subunit is higher than that of Gpp(NH)p. In analyzing a pyrophosphate molecule binding to domain II of the gamma subunit, we found a cleft that is very suitable for the acceptor stem of tRNA accommodation. It allows the suggestion of an alternative position for Met-tRNA i Met on the alphagamma intersubunit dimer, at variance with a recently published one. In the model reported here, the acceptor stem of the tRNAi is approximately perpendicular to that of tRNA in the ternary complex elongation factor Tu-Gpp(NH)p-tRNA. According to our analysis, the elbow and T stem of Met-tRNA i Met in this position should make extensive contact with the alpha subunit of aIF2. Thus, this model is in good agreement with experimental data showing that the alpha subunit of aIF2 is necessary for the stable interaction of aIF2gamma with Met-tRNA i Met. New insights into the interactions of the translation initiation factor 2 from archaea with guanine nucleotides and initiator tRNA.,Nikonov O, Stolboushkina E, Nikulin A, Hasenohrl D, Blasi U, Manstein DJ, Fedorov R, Garber M, Nikonov S J Mol Biol. 2007 Oct 19;373(2):328-36. Epub 2007 Aug 2. PMID:17825838[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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