8cah: Difference between revisions
m Protected "8cah" [edit=sysop:move=sysop] |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==Cryo-EM structure of native Otu2-bound ubiquitinated 43S pre-initiation complex== | ||
<StructureSection load='8cah' size='340' side='right'caption='[[8cah]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8cah]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_W303 Saccharomyces cerevisiae W303]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CAH FirstGlance]. <br> | |||
</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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'>[https://proteopedia.org/fgij/fg.htm?mol=8cah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cah OCA], [https://pdbe.org/8cah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cah RCSB], [https://www.ebi.ac.uk/pdbsum/8cah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cah ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A8H4BZ29_YEASX A0A8H4BZ29_YEASX] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.[HAMAP-Rule:MF_03002] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In actively translating 80S ribosomes the ribosomal protein eS7 of the 40S subunit is monoubiquitinated by the E3 ligase Not4 and deubiquitinated by Otu2 upon ribosomal subunit recycling. Despite its importance for translation efficiency the exact role and structural basis for this translational reset is poorly understood. Here, structural analysis by cryo-electron microscopy of native and reconstituted Otu2-bound ribosomal complexes reveals that Otu2 engages 40S subunits mainly between ribosome recycling and initiation stages. Otu2 binds to several sites on the intersubunit surface of the 40S that are not occupied by any other 40S-binding factors. This binding mode explains the discrimination against 80S ribosomes via the largely helical N-terminal domain of Otu2 as well as the specificity for mono-ubiquitinated eS7 on 40S. Collectively, this study reveals mechanistic insights into the Otu2-driven deubiquitination steps for translational reset during ribosome recycling/(re)initiation. | |||
Molecular basis for recognition and deubiquitination of 40S ribosomes by Otu2.,Ikeuchi K, Ivic N, Buschauer R, Cheng J, Frohlich T, Matsuo Y, Berninghausen O, Inada T, Becker T, Beckmann R Nat Commun. 2023 May 12;14(1):2730. doi: 10.1038/s41467-023-38161-w. PMID:37169754<ref>PMID:37169754</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8cah" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae W303]] | |||
[[Category: Becker T]] | |||
[[Category: Beckmann R]] | |||
[[Category: Berninghausen O]] | |||
[[Category: Buschauer R]] | |||
[[Category: Cheng J]] | |||
[[Category: Ikeuchi K]] | |||
Latest revision as of 07:02, 25 May 2023
Cryo-EM structure of native Otu2-bound ubiquitinated 43S pre-initiation complexCryo-EM structure of native Otu2-bound ubiquitinated 43S pre-initiation complex
Structural highlights
FunctionA0A8H4BZ29_YEASX Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.[HAMAP-Rule:MF_03002] Publication Abstract from PubMedIn actively translating 80S ribosomes the ribosomal protein eS7 of the 40S subunit is monoubiquitinated by the E3 ligase Not4 and deubiquitinated by Otu2 upon ribosomal subunit recycling. Despite its importance for translation efficiency the exact role and structural basis for this translational reset is poorly understood. Here, structural analysis by cryo-electron microscopy of native and reconstituted Otu2-bound ribosomal complexes reveals that Otu2 engages 40S subunits mainly between ribosome recycling and initiation stages. Otu2 binds to several sites on the intersubunit surface of the 40S that are not occupied by any other 40S-binding factors. This binding mode explains the discrimination against 80S ribosomes via the largely helical N-terminal domain of Otu2 as well as the specificity for mono-ubiquitinated eS7 on 40S. Collectively, this study reveals mechanistic insights into the Otu2-driven deubiquitination steps for translational reset during ribosome recycling/(re)initiation. Molecular basis for recognition and deubiquitination of 40S ribosomes by Otu2.,Ikeuchi K, Ivic N, Buschauer R, Cheng J, Frohlich T, Matsuo Y, Berninghausen O, Inada T, Becker T, Beckmann R Nat Commun. 2023 May 12;14(1):2730. doi: 10.1038/s41467-023-38161-w. PMID:37169754[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||