4crm: Difference between revisions

Latest revision as of 18:06, 8 September 2026

Cryo-EM of a pre-recycling complex with eRF1 and ABCE1

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Structural highlights

4crm is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 8.75Å
Ligands:	ADP, ATP, MG
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RLI1_YEAST Component of the multifactor complex (MFC) involved in translation initiation. Required for the binding of MFC to the 40S ribosome. Required for the processing and nuclear export of the 60S and 40S ribosomal subunits.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Termination and ribosome recycling are essential processes in translation. In eukaryotes, a stop codon in the ribosomal A site is decoded by a ternary complex consisting of release factors eRF1 and guanosine triphosphate (GTP)-bound eRF3. After GTP hydrolysis, eRF3 dissociates, and ABCE1 can bind to eRF1-loaded ribosomes to stimulate peptide release and ribosomal subunit dissociation. Here, we present cryoelectron microscopic (cryo-EM) structures of a pretermination complex containing eRF1-eRF3 and a termination/prerecycling complex containing eRF1-ABCE1. eRF1 undergoes drastic conformational changes: its central domain harboring the catalytically important GGQ loop is either packed against eRF3 or swung toward the peptidyl transferase center when bound to ABCE1. Additionally, in complex with eRF3, the N-terminal domain of eRF1 positions the conserved NIKS motif proximal to the stop codon, supporting its suggested role in decoding, yet it appears to be delocalized in the presence of ABCE1. These results suggest that stop codon decoding and peptide release can be uncoupled during termination.

Cryoelectron Microscopic Structures of Eukaryotic Translation Termination Complexes Containing eRF1-eRF3 or eRF1-ABCE1.,Preis A, Heuer A, Barrio-Garcia C, Hauser A, Eyler DE, Berninghausen O, Green R, Becker T, Beckmann R Cell Rep. 2014 Jul 10;8(1):59-65. doi: 10.1016/j.celrep.2014.04.058. Epub 2014, Jul 4. PMID:25001285^[4]

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

References

↑ Dong J, Lai R, Nielsen K, Fekete CA, Qiu H, Hinnebusch AG. The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly. J Biol Chem. 2004 Oct 1;279(40):42157-68. Epub 2004 Jul 23. PMID:15277527 doi:https://dx.doi.org/10.1074/jbc.M404502200
↑ Yarunin A, Panse VG, Petfalski E, Dez C, Tollervey D, Hurt EC. Functional link between ribosome formation and biogenesis of iron-sulfur proteins. EMBO J. 2005 Feb 9;24(3):580-8. Epub 2005 Jan 20. PMID:15660135 doi:https://dx.doi.org/10.1038/sj.emboj.7600540
↑ Kispal G, Sipos K, Lange H, Fekete Z, Bedekovics T, Janaky T, Bassler J, Aguilar Netz DJ, Balk J, Rotte C, Lill R. Biogenesis of cytosolic ribosomes requires the essential iron-sulphur protein Rli1p and mitochondria. EMBO J. 2005 Feb 9;24(3):589-98. Epub 2005 Jan 20. PMID:15660134 doi:https://dx.doi.org/10.1038/sj.emboj.7600541
↑ Preis A, Heuer A, Barrio-Garcia C, Hauser A, Eyler DE, Berninghausen O, Green R, Becker T, Beckmann R. Cryoelectron Microscopic Structures of Eukaryotic Translation Termination Complexes Containing eRF1-eRF3 or eRF1-ABCE1. Cell Rep. 2014 Jul 10;8(1):59-65. doi: 10.1016/j.celrep.2014.04.058. Epub 2014, Jul 4. PMID:25001285 doi:https://dx.doi.org/10.1016/j.celrep.2014.04.058

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Dong J, Lai R, Nielsen K, Fekete CA, Qiu H, Hinnebusch AG. The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly. J Biol Chem. 2004 Oct 1;279(40):42157-68. Epub 2004 Jul 23. PMID:15277527 doi:https://dx.doi.org/10.1074/jbc.M404502200

[2] Yarunin A, Panse VG, Petfalski E, Dez C, Tollervey D, Hurt EC. Functional link between ribosome formation and biogenesis of iron-sulfur proteins. EMBO J. 2005 Feb 9;24(3):580-8. Epub 2005 Jan 20. PMID:15660135 doi:https://dx.doi.org/10.1038/sj.emboj.7600540

[3] Kispal G, Sipos K, Lange H, Fekete Z, Bedekovics T, Janaky T, Bassler J, Aguilar Netz DJ, Balk J, Rotte C, Lill R. Biogenesis of cytosolic ribosomes requires the essential iron-sulphur protein Rli1p and mitochondria. EMBO J. 2005 Feb 9;24(3):589-98. Epub 2005 Jan 20. PMID:15660134 doi:https://dx.doi.org/10.1038/sj.emboj.7600541

[4] Preis A, Heuer A, Barrio-Garcia C, Hauser A, Eyler DE, Berninghausen O, Green R, Becker T, Beckmann R. Cryoelectron Microscopic Structures of Eukaryotic Translation Termination Complexes Containing eRF1-eRF3 or eRF1-ABCE1. Cell Rep. 2014 Jul 10;8(1):59-65. doi: 10.1016/j.celrep.2014.04.058. Epub 2014, Jul 4. PMID:25001285 doi:https://dx.doi.org/10.1016/j.celrep.2014.04.058

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[3]

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@@ Line 1: / Line 1: @@
 ==Cryo-EM of a pre-recycling complex with eRF1 and ABCE1==
-<StructureSection load='4crm' size='340' side='right' caption='[[4crm]], [[Resolution|resolution]] 8.75&Aring;' scene=''>
+<SX load='4crm' size='340' side='right' viewer='molstar' caption='[[4crm]], [[Resolution|resolution]] 8.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4crm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CRM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CRM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4crm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CRM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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]] 8.75&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4crn|4crn]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4crm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4crm OCA], [http://pdbe.org/4crm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4crm RCSB], [http://www.ebi.ac.uk/pdbsum/4crm 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=4crm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4crm OCA], [https://pdbe.org/4crm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4crm RCSB], [https://www.ebi.ac.uk/pdbsum/4crm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4crm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RLI1_YEAST RLI1_YEAST]] Component of the multifactor complex (MFC) involved in translation initiation. Required for the binding of MFC to the 40S ribosome. Required for the processing and nuclear export of the 60S and 40S ribosomal subunits.<ref>PMID:15277527</ref> <ref>PMID:15660135</ref> <ref>PMID:15660134</ref>  [[http://www.uniprot.org/uniprot/ERF1_YEAST ERF1_YEAST]] Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA (By similarity).<ref>PMID:7556078</ref>
+[https://www.uniprot.org/uniprot/RLI1_YEAST RLI1_YEAST] Component of the multifactor complex (MFC) involved in translation initiation. Required for the binding of MFC to the 40S ribosome. Required for the processing and nuclear export of the 60S and 40S ribosomal subunits.<ref>PMID:15277527</ref> <ref>PMID:15660135</ref> <ref>PMID:15660134</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 <references/>
 __TOC__
-</StructureSection>
+</SX>
-[[Category: Barrio-Garcia, C]]
+[[Category: Large Structures]]
-[[Category: Becker, T]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Beckmann, R]]
+[[Category: Barrio-Garcia C]]
-[[Category: Berninghausen, O]]
+[[Category: Becker T]]
-[[Category: Eyler, D]]
+[[Category: Beckmann R]]
-[[Category: Green, R]]
+[[Category: Berninghausen O]]
-[[Category: Hauser, A]]
+[[Category: Eyler D]]
-[[Category: Heuer, A]]
+[[Category: Green R]]
-[[Category: Preis, A]]
+[[Category: Hauser A]]
-[[Category: Recycling]]
+[[Category: Heuer A]]
-[[Category: Termination]]
+[[Category: Preis A]]
-[[Category: Translation]]

4crm: Difference between revisions

Latest revision as of 18:06, 8 September 2026

Cryo-EM of a pre-recycling complex with eRF1 and ABCE1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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