5me5

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of eiF4E from C. melo bound to a eIF4G peptide

Structural highlights

5me5 is a 2 chain structure with sequence from Cucumis melo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[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 PubMed

The 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.

References

↑ Nieto C, Morales M, Orjeda G, Clepet C, Monfort A, Sturbois B, Puigdomènech P, Pitrat M, Caboche M, Dogimont C, Garcia-Mas J, Aranda MA, Bendahmane A. An eIF4E allele confers resistance to an uncapped and non-polyadenylated RNA virus in melon. Plant J. 2006 Nov;48(3):452-62. PMID:17026540 doi:10.1111/j.1365-313X.2006.02885.x
↑ Miras M, Truniger V, Silva C, Verdaguer N, Aranda MA, Querol-Audi J. Structure of eIF4E in Complex with an eIF4G Peptide Supports a Universal Bipartite Binding Mode for Protein Translation. Plant Physiol. 2017 Jul;174(3):1476-1491. doi: 10.1104/pp.17.00193. Epub 2017 May, 18. PMID:28522457 doi:http://dx.doi.org/10.1104/pp.17.00193
↑ Nieto C, Morales M, Orjeda G, Clepet C, Monfort A, Sturbois B, Puigdomènech P, Pitrat M, Caboche M, Dogimont C, Garcia-Mas J, Aranda MA, Bendahmane A. An eIF4E allele confers resistance to an uncapped and non-polyadenylated RNA virus in melon. Plant J. 2006 Nov;48(3):452-62. PMID:17026540 doi:10.1111/j.1365-313X.2006.02885.x
↑ Miras M, Truniger V, Silva C, Verdaguer N, Aranda MA, Querol-Audi J. Structure of eIF4E in Complex with an eIF4G Peptide Supports a Universal Bipartite Binding Mode for Protein Translation. Plant Physiol. 2017 Jul;174(3):1476-1491. doi: 10.1104/pp.17.00193. Epub 2017 May, 18. PMID:28522457 doi:http://dx.doi.org/10.1104/pp.17.00193

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5me5"

@@ Line 3: / Line 3: @@
 <StructureSection load='5me5' size='340' side='right'caption='[[5me5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == 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 [http://proteopedia.org/fgij/fg.htm?mol=5ME5 FirstGlance]. <br>
+<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]] 1.9&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5me5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5me5 OCA], [http://pdbe.org/5me5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5me5 RCSB], [http://www.ebi.ac.uk/pdbsum/5me5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5me5 ProSAT]</span></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>
+<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>
+== 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;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 26: @@
 __TOC__
 </StructureSection>
+[[Category: Cucumis melo]]
 [[Category: Large Structures]]
-[[Category: Aranda-Regules, M]]
+[[Category: Aranda-Regules M]]
-[[Category: Miras, M]]
+[[Category: Miras M]]
-[[Category: Querol-Audi, J]]
+[[Category: Querol-Audi J]]
-[[Category: Silva, C]]
+[[Category: Silva C]]
-[[Category: Truniger, V]]
+[[Category: Truniger V]]
-[[Category: Verdaguer, N]]
+[[Category: Verdaguer N]]
-[[Category: Translation]]
-[[Category: Translation initiation eif4f complex]]

5me5

From Proteopedia

Current revision

Crystal Structure of eiF4E from C. melo bound to a eIF4G peptide

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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