9ynu

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Current revision (19:51, 4 December 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9ynu is ON HOLD until Paper Publication
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==Tra1 and core modules including core tip of ctSAGA complex==
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<StructureSection load='9ynu' size='340' side='right'caption='[[9ynu]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9ynu]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9YNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9YNU 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]] 3.2&#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=9ynu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ynu OCA], [https://pdbe.org/9ynu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ynu RCSB], [https://www.ebi.ac.uk/pdbsum/9ynu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ynu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/G0S6A1_CHATD G0S6A1_CHATD]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Spt-Ada-Gcn5 acetyltransferase (SAGA) complex, a 1.8 MDa multi-subunit assembly comprising 19 subunits, is required for RNA polymerase II transcription in eukaryotes. The complex consists of four modules: transcription-associated protein 1 (Tra1), core, deubiquitination (DUB), and histone acetyltransferase (HAT). Although the structures of the Tra1, core, and DUB modules have been determined, the overall architecture of the HAT module remained elusive due to its inherent flexibility. To address this, we conducted cryo-electron microscopy (cryo-EM) analyses on SAGA purified from the thermophilic fungus Chaetomium thermophilum, yielding structures of Tra1 and core modules at 2.6 A and three of the four HAT subunits at 3.7 A. The structure of the HAT module was informative about the aspects of histone acetylation and the interface of HAT-core modules, contradicting earlier AlphaFold predictions. Our structure-guided genetic and biochemical analyses confirmed the roles of Ada1 and Spt7 in anchoring the HAT module within the SAGA complex.
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Authors:
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Structure of the transcriptional co-activator SAGA complex, including the histone acetyltransferase module.,Mattoo RUH, Chen DH, Bushnell DA, Tamir S, Kornberg RD Mol Cell. 2025 Nov 18:S1097-2765(25)00866-4. doi: 10.1016/j.molcel.2025.10.025. PMID:41260211<ref>PMID:41260211</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 9ynu" 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: Chaetomium thermophilum]]
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[[Category: Large Structures]]
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[[Category: Bushnell DA]]
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[[Category: Chen DH]]
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[[Category: Kornberg RD]]
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[[Category: Mattoo RUH]]
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[[Category: Tamir S]]

Current revision

Tra1 and core modules including core tip of ctSAGA complex

PDB ID 9ynu

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