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8y0w
From Proteopedia
(Difference between revisions)
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==dormant ribosome with eIF5A, eEF2 and SERBP1== | ==dormant ribosome with eIF5A, eEF2 and SERBP1== | ||
| - | <StructureSection load='8y0w' size='340' side='right'caption='[[8y0w]]' scene=''> | + | <StructureSection load='8y0w' size='340' side='right'caption='[[8y0w]], [[Resolution|resolution]] 3.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8Y0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Y0W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[8y0w]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8Y0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Y0W FirstGlance]. <br> |
| - | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy</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]] 3.4Å</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=8y0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8y0w OCA], [https://pdbe.org/8y0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8y0w RCSB], [https://www.ebi.ac.uk/pdbsum/8y0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8y0w 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=8y0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8y0w OCA], [https://pdbe.org/8y0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8y0w RCSB], [https://www.ebi.ac.uk/pdbsum/8y0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8y0w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/IF5A1_HUMAN IF5A1_HUMAN] mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. With syntenin SDCBP, functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis. Regulates also TNF-alpha-mediated apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation. Also described as a cellular cofactor of human T-cell leukemia virus type I (HTLV-1) Rex protein and of human immunodeficiency virus type 1 (HIV-1) Rev protein, essential for mRNA export of retroviral transcripts.<ref>PMID:15371445</ref> <ref>PMID:15452064</ref> <ref>PMID:16987817</ref> <ref>PMID:17187778</ref> <ref>PMID:17360499</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Background: Dormant ribosomes are typically associated with preservation factors to protect themselves from degradation under stress conditions. Stm1/SERBP1 is one such protein that anchors the 40S and 60S subunits together. Several proteins and tRNAs bind to this complex as well, yet the molecular mechanisms remain unclear. Methods: Here, we reported the cryo-EM structures of five newly identified Stm1/SERBP1-bound ribosomes. Results: These structures highlighted that eIF5A, eEF2, and tRNA might bind to dormant ribosomes under stress to avoid their own degradation, thus facilitating protein synthesis upon the restoration of growth conditions. In addition, Ribo-seq data analysis reflected the upregulation of nutrient, metabolism, and external-stimulus-related pathways in the âstm1 strain, suggesting possible regulatory roles of Stm1. Discussion: The knowledge generated from the present work will facilitate in better understanding the molecular mechanism of dormant ribosomes. | ||
| + | |||
| + | Implication of Stm1 in the protection of eIF5A, eEF2 and tRNA through dormant ribosomes.,Du M, Li X, Dong W, Zeng F Front Mol Biosci. 2024 Apr 18;11:1395220. doi: 10.3389/fmolb.2024.1395220. , eCollection 2024. PMID:38698775<ref>PMID:38698775</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8y0w" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Du | + | [[Category: Du M]] |
| + | [[Category: Zeng F]] | ||
Current revision
dormant ribosome with eIF5A, eEF2 and SERBP1
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