6fc2: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='6fc2' size='340' side='right' caption='[[6fc2]], [[Resolution|resolution]] 1.92Å' scene=''> | <StructureSection load='6fc2' size='340' side='right' caption='[[6fc2]], [[Resolution|resolution]] 1.92Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6fc2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FC2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FC2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6fc2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FC2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FC2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDC33, TIF45, YOL139C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), EAP1, YKL204W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=6fc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fc2 OCA], [http://pdbe.org/6fc2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fc2 RCSB], [http://www.ebi.ac.uk/pdbsum/6fc2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fc2 ProSAT]</span></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=6fc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fc2 OCA], [http://pdbe.org/6fc2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fc2 RCSB], [http://www.ebi.ac.uk/pdbsum/6fc2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fc2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/IF4E_YEAST IF4E_YEAST]] 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. [[http://www.uniprot.org/uniprot/EAP1_YEAST EAP1_YEAST]] Can regulate translation through binding to eIF4E. Competes with eIF4G and p20 for binding to eIF4E in vivo and inhibits cap-dependent translation in vitro. Plays a role in cell growth and is implicated in the TOR signaling cascade. Functions independently of eIF4E to maintain genetic stability and to attenuate GCN4 translation upon TOR inactivation.<ref>PMID:10848587</ref> <ref>PMID:11114520</ref> <ref>PMID:15848184</ref> | [[http://www.uniprot.org/uniprot/IF4E_YEAST IF4E_YEAST]] 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. [[http://www.uniprot.org/uniprot/EAP1_YEAST EAP1_YEAST]] Can regulate translation through binding to eIF4E. Competes with eIF4G and p20 for binding to eIF4E in vivo and inhibits cap-dependent translation in vitro. Plays a role in cell growth and is implicated in the TOR signaling cascade. Functions independently of eIF4E to maintain genetic stability and to attenuate GCN4 translation upon TOR inactivation.<ref>PMID:10848587</ref> <ref>PMID:11114520</ref> <ref>PMID:15848184</ref> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The interaction of the eukaryotic initiation factor 4G (eIF4G) with the cap-binding protein eIF4E initiates cap-dependent translation and is regulated by the 4E-binding proteins (4E-BPs), which compete with eIF4G to repress translation. Metazoan eIF4G and 4E-BPs interact with eIF4E via canonical and non-canonical motifs that bind to the dorsal and lateral surface of eIF4E in a bipartite recognition mode. However, previous studies pointed to mechanistic differences in how fungi and metazoans regulate protein synthesis. We present crystal structures of the yeast eIF4E bound to two yeast 4E-BPs, p20 and Eap1p, as well as crystal structures of a fungal eIF4E-eIF4G complex. We demonstrate that the core principles of molecular recognition of eIF4E are in fact highly conserved among translational activators and repressors in eukaryotes. Finally, we reveal that highly specialized structural motifs do exist and serve to modulate the affinity of protein-protein interactions that regulate cap-dependent translation initiation in fungi. | |||
Structural motifs in eIF4G and 4E-BPs modulate their binding to eIF4E to regulate translation initiation in yeast.,Gruner S, Weber R, Peter D, Chung MY, Igreja C, Valkov E, Izaurralde E Nucleic Acids Res. 2018 Jul 27;46(13):6893-6908. doi: 10.1093/nar/gky542. PMID:30053226<ref>PMID:30053226</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6fc2" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Baker's yeast]] | |||
[[Category: Gruener, S]] | [[Category: Gruener, S]] | ||
[[Category: Valkov, E]] | [[Category: Valkov, E]] | ||
[[Category: Gene expression translation translational control 4e-binding protein]] | [[Category: Gene expression translation translational control 4e-binding protein]] | ||
[[Category: Translation]] | [[Category: Translation]] | ||
Latest revision as of 01:13, 10 August 2018
Crystal structure of the eIF4E-Eap1p complex from Saccharomyces cerevisiaeCrystal structure of the eIF4E-Eap1p complex from Saccharomyces cerevisiae
Structural highlights
Function[IF4E_YEAST] 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. [EAP1_YEAST] Can regulate translation through binding to eIF4E. Competes with eIF4G and p20 for binding to eIF4E in vivo and inhibits cap-dependent translation in vitro. Plays a role in cell growth and is implicated in the TOR signaling cascade. Functions independently of eIF4E to maintain genetic stability and to attenuate GCN4 translation upon TOR inactivation.[1] [2] [3] Publication Abstract from PubMedThe interaction of the eukaryotic initiation factor 4G (eIF4G) with the cap-binding protein eIF4E initiates cap-dependent translation and is regulated by the 4E-binding proteins (4E-BPs), which compete with eIF4G to repress translation. Metazoan eIF4G and 4E-BPs interact with eIF4E via canonical and non-canonical motifs that bind to the dorsal and lateral surface of eIF4E in a bipartite recognition mode. However, previous studies pointed to mechanistic differences in how fungi and metazoans regulate protein synthesis. We present crystal structures of the yeast eIF4E bound to two yeast 4E-BPs, p20 and Eap1p, as well as crystal structures of a fungal eIF4E-eIF4G complex. We demonstrate that the core principles of molecular recognition of eIF4E are in fact highly conserved among translational activators and repressors in eukaryotes. Finally, we reveal that highly specialized structural motifs do exist and serve to modulate the affinity of protein-protein interactions that regulate cap-dependent translation initiation in fungi. Structural motifs in eIF4G and 4E-BPs modulate their binding to eIF4E to regulate translation initiation in yeast.,Gruner S, Weber R, Peter D, Chung MY, Igreja C, Valkov E, Izaurralde E Nucleic Acids Res. 2018 Jul 27;46(13):6893-6908. doi: 10.1093/nar/gky542. PMID:30053226[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||