5me5: Difference between revisions
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<StructureSection load='5me5' size='340' side='right'caption='[[5me5]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5me5' size='340' side='right'caption='[[5me5]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5me5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ME5 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5me5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cucumis_melo Cucumis melo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ME5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ME5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.9Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5me5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5me5 OCA], [https://pdbe.org/5me5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5me5 RCSB], [https://www.ebi.ac.uk/pdbsum/5me5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5me5 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/IF4E1_CUCME IF4E1_CUCME] Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:17026540, PubMed:28522457). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (PubMed:17026540, PubMed:28522457). Key component of recessive resistance to potyviruses and Tombusviridae genus Carmovirus such as melon necrotic spot virus (MNSV) (PubMed:17026540).<ref>PMID:17026540</ref> <ref>PMID:28522457</ref> (Microbial infection) Susceptibility host factor required for viral infection by recruiting viral RNAs, including uncapped and non-polyadenylated RNA, to the host ribosomal complex via an interaction with viral genome-linked protein (VPg).<ref>PMID:17026540</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cucumis melo]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Aranda-Regules | [[Category: Aranda-Regules M]] | ||
[[Category: Miras | [[Category: Miras M]] | ||
[[Category: Querol-Audi | [[Category: Querol-Audi J]] | ||
[[Category: Silva | [[Category: Silva C]] | ||
[[Category: Truniger | [[Category: Truniger V]] | ||
[[Category: Verdaguer | [[Category: Verdaguer N]] | ||
Latest revision as of 21:40, 1 November 2023
Crystal Structure of eiF4E from C. melo bound to a eIF4G peptideCrystal Structure of eiF4E from C. melo bound to a eIF4G peptide
Structural highlights
FunctionIF4E1_CUCME Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:17026540, PubMed:28522457). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (PubMed:17026540, PubMed:28522457). Key component of recessive resistance to potyviruses and Tombusviridae genus Carmovirus such as melon necrotic spot virus (MNSV) (PubMed:17026540).[1] [2] (Microbial infection) Susceptibility host factor required for viral infection by recruiting viral RNAs, including uncapped and non-polyadenylated RNA, to the host ribosomal complex via an interaction with viral genome-linked protein (VPg).[3] Publication Abstract from PubMedThe association-dissociation of the cap-binding protein eukaryotic translation initiation factor 4E (eIF4E) with eIF4G is a key control step in eukaryotic translation. The paradigm on the eIF4E-eIF4G interaction states that eIF4G binds to the dorsal surface of eIF4E through a single canonical alpha-helical motif, while metazoan eIF4E-binding proteins (m4E-BPs) advantageously compete against eIF4G via bimodal interactions involving this canonical motif and a second noncanonical motif of the eIF4E surface. Metazoan eIF4Gs share this extended binding interface with m4E-BPs, with significant implications on the understanding of translation regulation and the design of therapeutic molecules. Here we show the high-resolution structure of melon (Cucumis melo) eIF4E in complex with a melon eIF4G peptide and propose the first eIF4E-eIF4G structural model for plants. Our structural data together with functional analyses demonstrate that plant eIF4G binds to eIF4E through both the canonical and noncanonical motifs, similarly to metazoan eIF4E-eIF4G complexes. As in the case of metazoan eIF4E-eIF4G, this may have very important practical implications, as plant eIF4E-eIF4G is also involved in a significant number of plant diseases. In light of our results, a universal eukaryotic bipartite mode of binding to eIF4E is proposed. Structure of eIF4E in Complex with an eIF4G Peptide Supports a Universal Bipartite Binding Mode for Protein Translation.,Miras M, Truniger V, Silva C, Verdaguer N, Aranda MA, Querol-Audi J Plant Physiol. 2017 Jul;174(3):1476-1491. doi: 10.1104/pp.17.00193. Epub 2017 May, 18. PMID:28522457[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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