2iu1: Difference between revisions

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New page: left|200px<br /> <applet load="2iu1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iu1, resolution 1.80Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:2iu1.gif|left|200px]]<br />
<applet load="2iu1" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2iu1, resolution 1.80&Aring;" />
'''CRYSTAL STRUCTURE OF EIF5 C-TERMINAL DOMAIN'''<br />


==Overview==
==Crystal structure of eIF5 C-terminal domain==
The carboxy-terminal domain (CTD) of eukaryotic initiation factor 5 (eIF5), plays a central role in the formation of the multifactor complex (MFC), an, important intermediate for the 43 S pre-initiation complex assembly. The, IF5-CTD interacts directly with the translation initiation factors eIF1, eIF2-beta, and eIF3c, thus forming together with eIF2 bound, Met-tRNA(i)(Met) the MFC. In this work we present the high resolution, crystal structure of eIF5-CTD. This domain of the protein is exclusively, composed out of alpha-helices and is homologous to the carboxy-terminal, domain of eIF2B-epsilon (eIF2Bepsilon-CTD). The most striking difference, in the two structures is an additional carboxy-terminal helix in eIF5. The, binding sites of eIF2-beta, eIF3 and eIF1 were mapped onto the structure., eIF2-beta and eIF3 bind to non-overlapping patches of negative and, positive electrostatic potential, respectively.
<StructureSection load='2iu1' size='340' side='right'caption='[[2iu1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2iu1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IU1 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]] 1.8&#8491;</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=2iu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iu1 OCA], [https://pdbe.org/2iu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iu1 RCSB], [https://www.ebi.ac.uk/pdbsum/2iu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iu1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IF5_HUMAN IF5_HUMAN] Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]).
== 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/iu/2iu1_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=2iu1 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The carboxy-terminal domain (CTD) of eukaryotic initiation factor 5 (eIF5) plays a central role in the formation of the multifactor complex (MFC), an important intermediate for the 43 S pre-initiation complex assembly. The IF5-CTD interacts directly with the translation initiation factors eIF1, eIF2-beta, and eIF3c, thus forming together with eIF2 bound Met-tRNA(i)(Met) the MFC. In this work we present the high resolution crystal structure of eIF5-CTD. This domain of the protein is exclusively composed out of alpha-helices and is homologous to the carboxy-terminal domain of eIF2B-epsilon (eIF2Bepsilon-CTD). The most striking difference in the two structures is an additional carboxy-terminal helix in eIF5. The binding sites of eIF2-beta, eIF3 and eIF1 were mapped onto the structure. eIF2-beta and eIF3 bind to non-overlapping patches of negative and positive electrostatic potential, respectively.


==About this Structure==
The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5.,Bieniossek C, Schutz P, Bumann M, Limacher A, Uson I, Baumann U J Mol Biol. 2006 Jul 7;360(2):457-65. Epub 2006 May 24. PMID:16781736<ref>PMID:16781736</ref>
2IU1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IU1 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5., Bieniossek C, Schutz P, Bumann M, Limacher A, Uson I, Baumann U, J Mol Biol. 2006 Jul 7;360(2):457-65. Epub 2006 May 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16781736 16781736]
</div>
<div class="pdbe-citations 2iu1" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Eukaryotic initiation factor 3D structures|Eukaryotic initiation factor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Baumann, U.]]
[[Category: Baumann U]]
[[Category: Bieniossek, C.]]
[[Category: Bieniossek C]]
[[Category: Schuetz, P.]]
[[Category: Schuetz P]]
[[Category: eif5]]
[[Category: gtp-binding]]
[[Category: initiation factor]]
[[Category: mfc]]
[[Category: nucleotide-binding]]
[[Category: phosphorylation]]
[[Category: protein biosynthesis]]
[[Category: transcription]]
[[Category: translation inititation]]
 
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Latest revision as of 09:29, 9 May 2024

Crystal structure of eIF5 C-terminal domain

2iu1, resolution 1.80Å

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