OCA at 05:45, 5 July 2023

2023-07-05T05:45:26Z

←Older revision		Revision as of 05:45, 5 July 2023
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-	'''Unreleased structure'''

-	The ~~entry~~ 8fz5 is ~~ON HOLD until Paper~~ Publication	+	==The PI31-free Bovine 20S proteasome==
		+	<StructureSection load='8fz5' size='340' side='right'caption='[[8fz5]], [[Resolution\|resolution]] 2.23Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8fz5]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FZ5 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]] 2.23Å</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=8fz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fz5 OCA], [https://pdbe.org/8fz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fz5 RCSB], [https://www.ebi.ac.uk/pdbsum/8fz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fz5 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/PSA6_BOVIN PSA6_BOVIN] Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).[UniProtKB:P60900]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Proteasome-catalyzed protein degradation mediates and regulates critical aspects of many cellular functions and is an important element of proteostasis in health and disease. Proteasome function is determined in part by the types of proteasome holoenzymes formed between the 20S core particle that catalyzes peptide bond hydrolysis and any of multiple regulatory proteins to which it binds. One of these regulators, PI31, was previously identified as an in vitro 20S proteasome inhibitor, but neither the molecular mechanism nor the possible physiologic significance of PI31-mediated proteasome inhibition has been clear. Here we report a high-resolution cryo-EM structure of the mammalian 20S proteasome in complex with PI31. The structure shows that two copies of the intrinsically disordered carboxyl terminus of PI31 are present in the central cavity of the closed-gate conformation of the proteasome and interact with proteasome catalytic sites in a manner that blocks proteolysis of substrates but resists their own degradation. The two inhibitory polypeptide chains appear to originate from PI31 monomers that enter the catalytic chamber from opposite ends of the 20S cylinder. We present evidence that PI31 can inhibit proteasome activity in mammalian cells and may serve regulatory functions for the control of cellular proteostasis.

-	~~Authors: Hsu, H.~~-C., Li, H.	+	Etaigh-resolution structure of mammalian PI31-20S proteasome complex reveals mechanism of proteasome inhibition.,Hsu HC, Wang J, Kjellgren A, Li H, DeMartino GN J Biol Chem. 2023 May 25;299(7):104862. doi: 10.1016/j.jbc.2023.104862. PMID:37236357<ref>PMID:37236357</ref>

-	~~Description: The PI31~~-~~free Bovine 20S proteasome~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
-	[[Category: ~~Li, H~~]]	+	<div class="pdbe-citations 8fz5" style="background-color:#fffaf0;"></div>
-	[[Category: Hsu, H.-C]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Bos taurus]]
		+	[[Category: Large Structures]]
		+	[[Category: Hsu H-C]]
		+	[[Category: Li H]]

OCA at 05:43, 8 March 2023

2023-03-08T05:43:21Z

←Older revision		Revision as of 05:43, 8 March 2023
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8fz5 is ON HOLD	+	The entry 8fz5 is ON HOLD until Paper Publication

	Authors: Hsu, H.-C., Li, H.		Authors: Hsu, H.-C., Li, H.

OCA: Protected "8fz5" [edit=sysop:move=sysop]

2023-02-08T05:12:59Z

Protected "8fz5" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:12, 8 February 2023

OCA: New page: '''Unreleased structure''' The entry 8fz5 is ON HOLD Authors: Hsu, H.-C., Li, H. Description: The PI31-free Bovine 20S proteasome Category: Unreleased Structures [[Category: Li, H]...

2023-02-08T05:12:58Z

New page: '''Unreleased structure''' The entry 8fz5 is ON HOLD Authors: Hsu, H.-C., Li, H. Description: The PI31-free Bovine 20S proteasome Category: Unreleased Structures [[Category: Li, H]...

New page

'''Unreleased structure'''

The entry 8fz5 is ON HOLD

Authors: Hsu, H.-C., Li, H.

Description: The PI31-free Bovine 20S proteasome
[[Category: Unreleased Structures]]
[[Category: Li, H]]
[[Category: Hsu, H.-C]]

8fz5 - Revision history

OCA at 05:45, 5 July 2023

OCA at 05:43, 8 March 2023

OCA: Protected "8fz5" [edit=sysop:move=sysop]

OCA: New page: '''Unreleased structure''' The entry 8fz5 is ON HOLD Authors: Hsu, H.-C., Li, H. Description: The PI31-free Bovine 20S proteasome Category: Unreleased Structures [[Category: Li, H]...