8qyj

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Current revision (05:28, 28 August 2024) (edit) (undo)
 
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<table><tr><td colspan='2'>[[8qyj]] 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=8QYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QYJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[8qyj]] 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=8QYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QYJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.73&#8491;</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]] 2.73&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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=8qyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qyj OCA], [https://pdbe.org/8qyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qyj RCSB], [https://www.ebi.ac.uk/pdbsum/8qyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qyj 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=8qyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qyj OCA], [https://pdbe.org/8qyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qyj RCSB], [https://www.ebi.ac.uk/pdbsum/8qyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qyj ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/PSMG2_HUMAN PSMG2_HUMAN] The disease may be caused by variants affecting the gene represented in this entry.
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/PSA2_HUMAN PSA2_HUMAN] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation.
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[https://www.uniprot.org/uniprot/PSMG2_HUMAN PSMG2_HUMAN] Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG1. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization.<ref>PMID:16251969</ref> <ref>PMID:17707236</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Dedicated assembly factors orchestrate the stepwise production of many molecular machines, including the 28-subunit proteasome core particle (CP) that mediates protein degradation. Here we report cryo-electron microscopy reconstructions of seven recombinant human subcomplexes that visualize all five chaperones and the three active site propeptides across a wide swath of the assembly pathway. Comparison of these chaperone-bound intermediates and a matching mature CP reveals molecular mechanisms determining the order of successive subunit additions, as well as how proteasome subcomplexes and assembly factors structurally adapt upon progressive subunit incorporation to stabilize intermediates, facilitate the formation of subsequent intermediates and ultimately rearrange to coordinate proteolytic activation with gated access to active sites. This work establishes a methodologic approach for structural analysis of multiprotein complex assembly intermediates, illuminates specific functions of assembly factors and reveals conceptual principles underlying human proteasome biogenesis, thus providing an explanation for many previous biochemical and genetic observations.
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Visualizing chaperone-mediated multistep assembly of the human 20S proteasome.,Adolf F, Du J, Goodall EA, Walsh RM Jr, Rawson S, von Gronau S, Harper JW, Hanna J, Schulman BA Nat Struct Mol Biol. 2024 Aug;31(8):1176-1188. doi: 10.1038/s41594-024-01268-9. , Epub 2024 Apr 10. PMID:38600324<ref>PMID:38600324</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8qyj" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Human 20S proteasome assembly structure 1

PDB ID 8qyj

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