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[[Image:2iu1.gif|left|200px]]
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{{STRUCTURE_2iu1|  PDB=2iu1  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF EIF5 C-TERMINAL DOMAIN'''


==Crystal structure of eIF5 C-terminal domain==
<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.


==Overview==
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>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2IU1 is a [[Single protein]] structure of sequence from [http://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].
</div>
<div class="pdbe-citations 2iu1" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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://www.ncbi.nlm.nih.gov/pubmed/16781736 16781736]
*[[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]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 07:52:40 2008''