7qyb: Difference between revisions
New page: '''Unreleased structure''' The entry 7qyb is ON HOLD Authors: Zhu, Y., Lu, Y. Description: Proteasome-ZFAND5 Complex Z-C state Category: Unreleased Structures Category: Lu, Y [... |
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==Proteasome-ZFAND5 Complex Z-C state== | |||
<StructureSection load='7qyb' size='340' side='right'caption='[[7qyb]], [[Resolution|resolution]] 4.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7qyb]] 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=7QYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QYB 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]] 4.1Å</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=7qyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qyb OCA], [https://pdbe.org/7qyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qyb RCSB], [https://www.ebi.ac.uk/pdbsum/7qyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qyb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PSMD3_HUMAN PSMD3_HUMAN] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Various hormones, kinases, and stressors (fasting, heat shock) stimulate 26S proteasome activity. To understand how its capacity to degrade ubiquitylated proteins can increase, we studied mouse ZFAND5, which promotes protein degradation during muscle atrophy. Cryo-electron microscopy showed that ZFAND5 induces large conformational changes in the 19S regulatory particle. ZFAND5's AN1 Zn-finger domain interacts with the Rpt5 ATPase and its C terminus with Rpt1 ATPase and Rpn1, a ubiquitin-binding subunit. Upon proteasome binding, ZFAND5 widens the entrance of the substrate translocation channel, yet it associates only transiently with the proteasome. Dissociation of ZFAND5 then stimulates opening of the 20S proteasome gate. Using single-molecule microscopy, we showed that ZFAND5 binds ubiquitylated substrates, prolongs their association with proteasomes, and increases the likelihood that bound substrates undergo degradation, even though ZFAND5 dissociates before substrate deubiquitylation. These changes in proteasome conformation and reaction cycle can explain the accelerated degradation and suggest how other proteasome activators may stimulate proteolysis. | |||
Molecular mechanism for activation of the 26S proteasome by ZFAND5.,Lee D, Zhu Y, Colson L, Wang X, Chen S, Tkacik E, Huang L, Ouyang Q, Goldberg AL, Lu Y Mol Cell. 2023 Aug 17;83(16):2959-2975.e7. doi: 10.1016/j.molcel.2023.07.023. PMID:37595557<ref>PMID:37595557</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Lu | <div class="pdbe-citations 7qyb" style="background-color:#fffaf0;"></div> | ||
[[Category: Zhu | |||
==See Also== | |||
*[[Proteasome 3D structures|Proteasome 3D structures]] | |||
*[[Thyroid hormone receptor 3D structures|Thyroid hormone receptor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Lu Y]] | |||
[[Category: Zhu Y]] | |||
Latest revision as of 08:48, 4 September 2024
Proteasome-ZFAND5 Complex Z-C stateProteasome-ZFAND5 Complex Z-C state
Structural highlights
FunctionPSMD3_HUMAN Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Publication Abstract from PubMedVarious hormones, kinases, and stressors (fasting, heat shock) stimulate 26S proteasome activity. To understand how its capacity to degrade ubiquitylated proteins can increase, we studied mouse ZFAND5, which promotes protein degradation during muscle atrophy. Cryo-electron microscopy showed that ZFAND5 induces large conformational changes in the 19S regulatory particle. ZFAND5's AN1 Zn-finger domain interacts with the Rpt5 ATPase and its C terminus with Rpt1 ATPase and Rpn1, a ubiquitin-binding subunit. Upon proteasome binding, ZFAND5 widens the entrance of the substrate translocation channel, yet it associates only transiently with the proteasome. Dissociation of ZFAND5 then stimulates opening of the 20S proteasome gate. Using single-molecule microscopy, we showed that ZFAND5 binds ubiquitylated substrates, prolongs their association with proteasomes, and increases the likelihood that bound substrates undergo degradation, even though ZFAND5 dissociates before substrate deubiquitylation. These changes in proteasome conformation and reaction cycle can explain the accelerated degradation and suggest how other proteasome activators may stimulate proteolysis. Molecular mechanism for activation of the 26S proteasome by ZFAND5.,Lee D, Zhu Y, Colson L, Wang X, Chen S, Tkacik E, Huang L, Ouyang Q, Goldberg AL, Lu Y Mol Cell. 2023 Aug 17;83(16):2959-2975.e7. doi: 10.1016/j.molcel.2023.07.023. PMID:37595557[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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