8b3g

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m (Protected "8b3g" [edit=sysop:move=sysop])
Current revision (05:32, 4 September 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8b3g is ON HOLD
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==C(N)RL4CSA-UVSSA-E2-ubiquitin complex.==
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<StructureSection load='8b3g' size='340' side='right'caption='[[8b3g]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8b3g]] is a 8 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=8B3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8B3G FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.4&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8b3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8b3g OCA], [https://pdbe.org/8b3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8b3g RCSB], [https://www.ebi.ac.uk/pdbsum/8b3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8b3g ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A6P5C4T4_BOSIN A0A6P5C4T4_BOSIN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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During transcription-coupled DNA repair (TCR), RNA polymerase II (Pol II) transitions from a transcriptionally active state to an arrested state that allows for removal of DNA lesions. This transition requires site-specific ubiquitylation of Pol II by the CRL4(CSA) ubiquitin ligase, a process that is facilitated by ELOF1 in an unknown way. Using cryogenic electron microscopy, biochemical assays and cell biology approaches, we found that ELOF1 serves as an adaptor to stably position UVSSA and CRL4(CSA) on arrested Pol II, leading to ligase neddylation and activation of Pol II ubiquitylation. In the presence of ELOF1, a transcription factor IIS (TFIIS)-like element in UVSSA gets ordered and extends through the Pol II pore, thus preventing reactivation of Pol II by TFIIS. Our results provide the structural basis for Pol II ubiquitylation and inactivation in TCR.
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Authors:
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Structural basis for RNA polymerase II ubiquitylation and inactivation in transcription-coupled repair.,Kokic G, Yakoub G, van den Heuvel D, Wondergem AP, van der Meer PJ, van der Weegen Y, Chernev A, Fianu I, Fokkens TJ, Lorenz S, Urlaub H, Cramer P, Luijsterburg MS Nat Struct Mol Biol. 2024 Mar;31(3):536-547. doi: 10.1038/s41594-023-01207-0. , Epub 2024 Feb 5. PMID:38316879<ref>PMID:38316879</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8b3g" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Cramer P]]
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[[Category: Kokic G]]

Current revision

C(N)RL4CSA-UVSSA-E2-ubiquitin complex.

PDB ID 8b3g

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