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| | <StructureSection load='2iu1' size='340' side='right'caption='[[2iu1]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='2iu1' size='340' side='right'caption='[[2iu1]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2iu1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IU1 FirstGlance]. <br> | + | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iu1 OCA], [http://pdbe.org/2iu1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iu1 RCSB], [http://www.ebi.ac.uk/pdbsum/2iu1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iu1 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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]). | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Eukaryotic initiation factor|Eukaryotic initiation factor]] | + | *[[Eukaryotic initiation factor 3D structures|Eukaryotic initiation factor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[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]]
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| - | [[Category: Mfc]]
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| - | [[Category: Nucleotide-binding]]
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| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Protein biosynthesis]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Translation inititation]]
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| Structural highlights
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.
See Also
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
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