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2iu1

From Proteopedia

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Current revision

Crystal structure of eIF5 C-terminal domain

Structural highlights

2iu1 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bieniossek C, Schutz P, Bumann M, Limacher A, Uson I, Baumann U. The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5. J Mol Biol. 2006 Jul 7;360(2):457-65. Epub 2006 May 24. PMID:16781736 doi:http://dx.doi.org/10.1016/j.jmb.2006.05.021

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2iu1"

Categories: Homo sapiens | Large Structures | Baumann U | Bieniossek C | Schuetz P

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:2iu1.png|left|200px]]
-<!--
+==Crystal structure of eIF5 C-terminal domain==
-The line below this paragraph, containing "STRUCTURE_2iu1", creates the "Structure Box" on the page.
+<StructureSection load='2iu1' size='340' side='right'caption='[[2iu1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
-{{STRUCTURE_2iu1|  PDB=2iu1  |  SCENE=  }}
+</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.
-===CRYSTAL STRUCTURE OF EIF5 C-TERMINAL DOMAIN===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2iu1" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16781736}}, adds the Publication Abstract to the page
+*[[Eukaryotic initiation factor 3D structures|Eukaryotic initiation factor 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16781736 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16781736}}
+__TOC__
+</StructureSection>
-==About this Structure==
-IU1 is a 1 chain 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].
-==Reference==
-<ref group="xtra">PMID:16781736</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Baumann, U.]]
+[[Category: Large Structures]]
-[[Category: Bieniossek, C.]]
+[[Category: Baumann U]]
-[[Category: Schuetz, P.]]
+[[Category: Bieniossek C]]
-[[Category: Eif5]]
+[[Category: Schuetz P]]
-[[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 Mon Feb 16 22:30:50 2009''

2iu1

From Proteopedia

Current revision

Crystal structure of eIF5 C-terminal domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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