8aaf: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8aaf]] is a 10 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=8AAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AAF FirstGlance]. <br> | <table><tr><td colspan='2'>[[8aaf]] is a 10 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=8AAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AAF FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5CT:HYPUSINE'>5CT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</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">Electron Microscopy, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5CT:HYPUSINE'>5CT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</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=8aaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aaf OCA], [https://pdbe.org/8aaf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aaf RCSB], [https://www.ebi.ac.uk/pdbsum/8aaf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aaf ProSAT]</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=8aaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aaf OCA], [https://pdbe.org/8aaf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aaf RCSB], [https://www.ebi.ac.uk/pdbsum/8aaf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aaf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 14:52, 23 October 2024
Yeast RQC complex in state GYeast RQC complex in state G
Structural highlights
FunctionPublication Abstract from PubMedRibosome-associated quality control (RQC) is a conserved process degrading potentially toxic truncated nascent peptides whose malfunction underlies neurodegeneration and proteostasis decline in aging. During RQC, dissociation of stalled ribosomes is followed by elongation of the nascent peptide with alanine and threonine residues, driven by Rqc2 independently of mRNA, the small ribosomal subunit and guanosine triphosphate (GTP)-hydrolyzing factors. The resulting CAT tails (carboxy-terminal tails) and ubiquitination by Ltn1 mark nascent peptides for proteasomal degradation. Here we present ten cryogenic electron microscopy (cryo-EM) structures, revealing the mechanistic basis of individual steps of the CAT tailing cycle covering initiation, decoding, peptidyl transfer, and tRNA translocation. We discovered eIF5A as a crucial eukaryotic RQC factor enabling peptidyl transfer. Moreover, we observed dynamic behavior of RQC factors and tRNAs allowing for processivity of the CAT tailing cycle without additional energy input. Together, these results elucidate key differences as well as common principles between CAT tailing and canonical translation. Molecular basis of eIF5A-dependent CAT tailing in eukaryotic ribosome-associated quality control.,Tesina P, Ebine S, Buschauer R, Thoms M, Matsuo Y, Inada T, Beckmann R Mol Cell. 2023 Feb 16;83(4):607-621.e4. doi: 10.1016/j.molcel.2023.01.020. PMID:36804914[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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