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6o80

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Current revision (14:50, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6o80' size='340' side='right'caption='[[6o80]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='6o80' size='340' side='right'caption='[[6o80]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6o80]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trycr Trycr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O80 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O80 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6o80]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_cruzi Trypanosoma cruzi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O80 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MGP:7-METHYL-GUANOSINE-5-TRIPHOSPHATE'>MGP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6o7y|6o7y]], [[6o7z|6o7z]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MGP:7-METHYL-GUANOSINE-5-TRIPHOSPHATE'>MGP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C4B63_13g194 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5693 TRYCR])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6o80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o80 OCA], [https://pdbe.org/6o80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o80 RCSB], [https://www.ebi.ac.uk/pdbsum/6o80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o80 ProSAT]</span></td></tr>
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<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=6o80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o80 OCA], [http://pdbe.org/6o80 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o80 RCSB], [http://www.ebi.ac.uk/pdbsum/6o80 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o80 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A2V2VRR6_TRYCR A0A2V2VRR6_TRYCR]
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Association of the initiation factor eIF4E with the mRNA cap structure is a key step for translation. Trypanosomatids present six eIF4E homologues, showing a low conservation and also differing significantly from the IF4Es of multicellular eukaryotes. On the mRNA side, while in most eukaryotes the mRNA contains cap-0 (7-methyl-GTP), the trypanosomatid mRNA features a cap-4, which is formed by a cap-0, followed by the AACU sequence containing 2'-O-ribose methylations and base methylations on nucleotides 1 and 4. The studies on eIF4E-cap-4 interaction have been hindered by the difficulty to synthesize this rather elaborated cap-4 sequence. To overcome this problem, we applied a liquid-phase oligonucleotide synthesis strategy and describe for the first time the crystal structure of a trypanosomatid eIF4E (T. cruzi EIF4E5) in complex with cap-4. The TcEIF4E5-cap-4 structure allowed a detailed description of the binding mechanism, revealing the interaction mode for the AACU sequence, with the bases packed in a parallel stacking conformation and involved, together with the methyl groups, in hydrophobic contacts with the protein. This binding mechanism evidences a distinct cap interaction mode in comparison with previously described eIF4E structures and may account for the difference of TcEIF4E5-cap-4 dissociation constant in comparison with other eIF4E homologues.
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Crystal structure of the Trypanosoma cruzi EIF4E5 translation factor homologue in complex with mRNA cap-4.,Reolon LW, Vichier-Guerre S, de Matos BM, Dugue L, Assuncao TRDS, Tonin Zanchin NI, Pochet S, Guimaraes BG Nucleic Acids Res. 2019 May 8. pii: 5486744. doi: 10.1093/nar/gkz339. PMID:31066441<ref>PMID:31066441</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6o80" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Trycr]]
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[[Category: Trypanosoma cruzi]]
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[[Category: Guimaraes, B G]]
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[[Category: Guimaraes BG]]
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[[Category: Reolon, L W]]
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[[Category: Reolon LW]]
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[[Category: Rna binding protein]]
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[[Category: Translation initiation factor]]
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Current revision

Trypanosoma cruzi EIF4E5 translation initiation factor in complex with m7GTP

PDB ID 6o80

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