View source for 7v5m


==20S+monoUb-CyclinB1-NT (S2)==
<StructureSection load='7v5m' size='340' side='right'caption='[[7v5m]], [[Resolution|resolution]] 3.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7v5m]] is a 20 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=7V5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V5M 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]] 3.88&#8491;</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=7v5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v5m OCA], [https://pdbe.org/7v5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v5m RCSB], [https://www.ebi.ac.uk/pdbsum/7v5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v5m ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PSA6_HUMAN PSA6_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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The proteasome, the primary protease for ubiquitin-dependent proteolysis in eukaryotes, is usually found as a mixture of 30S, 26S, and 20S complexes. These complexes have common catalytic sites, which makes it challenging to determine their distinctive roles in intracellular proteolysis. Here, we chemically synthesize a panel of homogenous ubiquitinated proteins, and use them to compare 20S and 26S proteasomes with respect to substrate selection and peptide-product generation. We show that 20S proteasomes can degrade the ubiquitin tag along with the conjugated substrate. Ubiquitin remnants on branched peptide products identified by LC-MS/MS, and flexibility in the 20S gate observed by cryo-EM, reflect the ability of the 20S proteasome to proteolyze an isopeptide-linked ubiquitin-conjugate. Peptidomics identifies proteasome-trapped ubiquitin-derived peptides and peptides of potential 20S substrates in Hi20S cells, hypoxic cells, and human failing-heart. Moreover, elevated levels of 20S proteasomes appear to contribute to cell survival under stress associated with damaged proteins.

The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag.,Sahu I, Mali SM, Sulkshane P, Xu C, Rozenberg A, Morag R, Sahoo MP, Singh SK, Ding Z, Wang Y, Day S, Cong Y, Kleifeld O, Brik A, Glickman MH Nat Commun. 2021 Oct 26;12(1):6173. doi: 10.1038/s41467-021-26427-0. PMID:34702852<ref>PMID:34702852</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7v5m" style="background-color:#fffaf0;"></div>

==See Also==
*[[Proteasome 3D structures|Proteasome 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Cong Y]]
[[Category: Xu C]]