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5abx

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Complex of C. elegans eIF4E-3 with the 4E-binding protein Mextli and cap analog

Structural highlights

5abx is a 2 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.66Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IF4E3_CAEEL 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. All 5 eIF4E proteins bind monomethyl cap structures. Only ife-1, ife-2 and ife-5 bind trimethyl cap structures which result from trans-splicing. Translation of trimethyl cap structure mRNAs may be regulated by intracellular redox state; disulfide bonds change the width and depth of the cap-binding cavity determining selectivity to mRNA caps. Ife-3 is essential for viability.^[1] ^[2] ^[3]

Publication Abstract from PubMed

The eIF4E-binding proteins (4E-BPs) are a diverse class of translation regulators that share a canonical eIF4E-binding motif (4E-BM) with eIF4G. Consequently, they compete with eIF4G for binding to eIF4E, thereby inhibiting translation initiation. Mextli (Mxt) is an unusual 4E-BP that promotes translation by also interacting with eIF3. Here we present the crystal structures of the eIF4E-binding regions of the Drosophila melanogaster (Dm) and Caenorhabditis elegans (Ce) Mxt proteins in complex with eIF4E in the cap-bound and cap-free states. The structures reveal unexpected evolutionary plasticity in the eIF4E-binding mode, with a classical bipartite interface for Ce Mxt and a novel tripartite interface for Dm Mxt. Both interfaces comprise a canonical helix and a noncanonical helix that engage the dorsal and lateral surfaces of eIF4E, respectively. Remarkably, Dm Mxt contains a C-terminal auxiliary helix that lies anti-parallel to the canonical helix on the eIF4E dorsal surface. In contrast to the eIF4G and Ce Mxt complexes, the Dm eIF4E-Mxt complexes are resistant to competition by bipartite 4E-BPs, suggesting that Dm Mxt can bind eIF4E when eIF4G binding is inhibited. Our results uncovered unexpected diversity in the binding modes of 4E-BPs, resulting in eIF4E complexes that display differential sensitivity to 4E-BP regulation.

Mextli proteins use both canonical bipartite and novel tripartite binding modes to form eIF4E complexes that display differential sensitivity to 4E-BP regulation.,Peter D, Weber R, Kone C, Chung MY, Ebertsch L, Truffault V, Weichenrieder O, Igreja C, Izaurralde E Genes Dev. 2015 Aug 20. PMID:26294658^[4]

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

References

↑ Keiper BD, Lamphear BJ, Deshpande AM, Jankowska-Anyszka M, Aamodt EJ, Blumenthal T, Rhoads RE. Functional characterization of five eIF4E isoforms in Caenorhabditis elegans. J Biol Chem. 2000 Apr 7;275(14):10590-6. PMID:10744754
↑ Stachelska A, Wieczorek Z, Ruszczynska K, Stolarski R, Pietrzak M, Lamphear BJ, Rhoads RE, Darzynkiewicz E, Jankowska-Anyszka M. Interaction of three Caenorhabditis elegans isoforms of translation initiation factor eIF4E with mono- and trimethylated mRNA 5' cap analogues. Acta Biochim Pol. 2002;49(3):671-82. PMID:12422237
↑ Jankowska-Anyszka M, Lamphear BJ, Aamodt EJ, Harrington T, Darzynkiewicz E, Stolarski R, Rhoads RE. Multiple isoforms of eukaryotic protein synthesis initiation factor 4E in Caenorhabditis elegans can distinguish between mono- and trimethylated mRNA cap structures. J Biol Chem. 1998 Apr 24;273(17):10538-42. PMID:9553113
↑ Peter D, Weber R, Kone C, Chung MY, Ebertsch L, Truffault V, Weichenrieder O, Igreja C, Izaurralde E. Mextli proteins use both canonical bipartite and novel tripartite binding modes to form eIF4E complexes that display differential sensitivity to 4E-BP regulation. Genes Dev. 2015 Aug 20. PMID:26294658 doi:http://dx.doi.org/10.1101/gad.269068.115

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/5abx"

Categories: Caenorhabditis elegans | Large Structures | Peter D | Weichenrieder O

@@ Line 1: / Line 1: @@
 ==Complex of C. elegans eIF4E-3 with the 4E-binding protein Mextli and cap analog==
-<StructureSection load='5abx' size='340' side='right' caption='[[5abx]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
+<StructureSection load='5abx' size='340' side='right'caption='[[5abx]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5abx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ABX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ABX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5abx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ABX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ABX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MGP:7-METHYL-GUANOSINE-5-TRIPHOSPHATE'>MGP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.66&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5abu|5abu]], [[5abv|5abv]], [[5aby|5aby]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MGP:7-METHYL-GUANOSINE-5-TRIPHOSPHATE'>MGP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5abx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5abx OCA], [http://pdbe.org/5abx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5abx RCSB], [http://www.ebi.ac.uk/pdbsum/5abx PDBsum]</span></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=5abx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5abx OCA], [https://pdbe.org/5abx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5abx RCSB], [https://www.ebi.ac.uk/pdbsum/5abx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5abx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/IF4E3_CAEEL IF4E3_CAEEL]] 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. All 5 eIF4E proteins bind monomethyl cap structures. Only ife-1, ife-2 and ife-5 bind trimethyl cap structures which result from trans-splicing. Translation of trimethyl cap structure mRNAs may be regulated by intracellular redox state; disulfide bonds change the width and depth of the cap-binding cavity determining selectivity to mRNA caps. Ife-3 is essential for viability.<ref>PMID:10744754</ref> <ref>PMID:12422237</ref> <ref>PMID:9553113</ref>
+[https://www.uniprot.org/uniprot/IF4E3_CAEEL IF4E3_CAEEL] 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. All 5 eIF4E proteins bind monomethyl cap structures. Only ife-1, ife-2 and ife-5 bind trimethyl cap structures which result from trans-splicing. Translation of trimethyl cap structure mRNAs may be regulated by intracellular redox state; disulfide bonds change the width and depth of the cap-binding cavity determining selectivity to mRNA caps. Ife-3 is essential for viability.<ref>PMID:10744754</ref> <ref>PMID:12422237</ref> <ref>PMID:9553113</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 5abx" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Eukaryotic initiation factor 3D structures|Eukaryotic initiation factor 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Peter, D]]
+[[Category: Caenorhabditis elegans]]
-[[Category: Weichenrieder, O]]
+[[Category: Large Structures]]
-[[Category: 4e binding protein]]
+[[Category: Peter D]]
-[[Category: Cap binding protein]]
+[[Category: Weichenrieder O]]
-[[Category: Gene regulation]]
-[[Category: Translation]]

5abx

From Proteopedia

Current revision

Complex of C. elegans eIF4E-3 with the 4E-binding protein Mextli and cap analog

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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