5k0y: Difference between revisions

Latest revision as of 18:16, 7 May 2025

m48S late-stage initiation complex, purified from rabbit reticulocytes lysates, displaying eIF2 ternary complex and eIF3 i and g subunits relocated to the intersubunit face

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Structural highlights

5k0y is a 10 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 5.8Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

G1T2G4_RABIT

Publication Abstract from PubMed

mRNA translation initiation in eukaryotes requires the cooperation of a dozen eukaryotic initiation factors (eIFs) forming several complexes, which leads to mRNA attachment to the small ribosomal 40S subunit, mRNA scanning for start codon, and accommodation of initiator tRNA at the 40S P site. eIF3, composed of 13 subunits, 8 core (a, c, e, f, h, l, k, and m) and 5 peripheral (b, d, g, i, and j), plays a central role during this process. Here we report a cryo-electron microscopy structure of a mammalian 48S initiation complex at 5.8 A resolution. It shows the relocation of subunits eIF3i and eIF3g to the 40S intersubunit face on the GTPase binding site, at a late stage in initiation. On the basis of a previous study, we demonstrate the relocation of eIF3b to the 40S intersubunit face, binding below the eIF2-Met-tRNAiMet ternary complex upon mRNA attachment. Our analysis reveals the deep rearrangement of eIF3 and unravels the molecular mechanism underlying eIF3 function in mRNA scanning and timing of ribosomal subunit joining.

eIF3 Peripheral Subunits Rearrangement after mRNA Binding and Start-Codon Recognition.,Simonetti A, Brito Querido J, Myasnikov AG, Mancera-Martinez E, Renaud A, Kuhn L, Hashem Y Mol Cell. 2016 Jun 29. pii: S1097-2765(16)30197-6. doi:, 10.1016/j.molcel.2016.05.033. PMID:27373335^[1]

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

References

↑ Simonetti A, Brito Querido J, Myasnikov AG, Mancera-Martinez E, Renaud A, Kuhn L, Hashem Y. eIF3 Peripheral Subunits Rearrangement after mRNA Binding and Start-Codon Recognition. Mol Cell. 2016 Jun 29. pii: S1097-2765(16)30197-6. doi:, 10.1016/j.molcel.2016.05.033. PMID:27373335 doi:https://dx.doi.org/10.1016/j.molcel.2016.05.033

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OCA

[1] Simonetti A, Brito Querido J, Myasnikov AG, Mancera-Martinez E, Renaud A, Kuhn L, Hashem Y. eIF3 Peripheral Subunits Rearrangement after mRNA Binding and Start-Codon Recognition. Mol Cell. 2016 Jun 29. pii: S1097-2765(16)30197-6. doi:, 10.1016/j.molcel.2016.05.033. PMID:27373335 doi:https://dx.doi.org/10.1016/j.molcel.2016.05.033

[1]

@@ Line 1: / Line 1: @@
-{{Large structure}}
 ==m48S late-stage initiation complex, purified from rabbit reticulocytes lysates, displaying eIF2 ternary complex and eIF3 i and g subunits relocated to the intersubunit face==
-<StructureSection load='5k0y' size='340' side='right' caption='[[5k0y]], [[Resolution|resolution]] 5.80&Aring;' scene=''>
+<SX load='5k0y' size='340' side='right' viewer='molstar' caption='[[5k0y]], [[Resolution|resolution]] 5.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5k0y]] is a 42 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K0Y FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5k0y]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K0Y FirstGlance]. <br>
-</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=5k0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k0y OCA], [http://pdbe.org/5k0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k0y RCSB], [http://www.ebi.ac.uk/pdbsum/5k0y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k0y ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.8&#8491;</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=5k0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k0y OCA], [https://pdbe.org/5k0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k0y RCSB], [https://www.ebi.ac.uk/pdbsum/5k0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k0y ProSAT]</span></td></tr>
 </table>
-{{Large structure}}
 == Function ==
-[[http://www.uniprot.org/uniprot/EIF3I_RABIT EIF3I_RABIT]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.[HAMAP-Rule:MF_03008] [[http://www.uniprot.org/uniprot/G1TN72_RABIT G1TN72_RABIT]] May play a role during erythropoiesis through regulation of transcription factor DDIT3 (By similarity).[HAMAP-Rule:MF_03122] [[http://www.uniprot.org/uniprot/EIF3G_HUMAN EIF3G_HUMAN]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. This subunit can bind 18S rRNA.
+[https://www.uniprot.org/uniprot/G1T2G4_RABIT G1T2G4_RABIT]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 18: @@
 </div>
 <div class="pdbe-citations 5k0y" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Eukaryotic initiation factor 3D structures|Eukaryotic initiation factor 3D structures]]
+*[[3D sructureseceptor for activated protein kinase C 1|3D sructureseceptor for activated protein kinase C 1]]
 == References ==
 <references/>
 __TOC__
-</StructureSection>
+</SX>
-[[Category: Hashem, Y]]
+[[Category: Large Structures]]
-[[Category: Kuhn, L]]
+[[Category: Oryctolagus cuniculus]]
-[[Category: Mancera-Martinez, E]]
+[[Category: Brito Querido J]]
-[[Category: Myasnikov, A G]]
+[[Category: Hashem Y]]
-[[Category: Querido, J Brito]]
+[[Category: Kuhn L]]
-[[Category: Renaud, A]]
+[[Category: Mancera-Martinez E]]
-[[Category: Simonetti, A]]
+[[Category: Myasnikov AG]]
-[[Category: Cryo-em]]
+[[Category: Renaud A]]
-[[Category: Eif3 peripheral subunit]]
+[[Category: Simonetti A]]
-[[Category: Eukaryotic translation initiation]]
-[[Category: Ribosome]]
-[[Category: Translation]]

5k0y: Difference between revisions

Latest revision as of 18:16, 7 May 2025

m48S late-stage initiation complex, purified from rabbit reticulocytes lysates, displaying eIF2 ternary complex and eIF3 i and g subunits relocated to the intersubunit face

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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