8ygc

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Current revision (07:59, 5 March 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8ygc is ON HOLD until Paper Publication
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==The Dimer Structure of DSR2-SPR==
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<StructureSection load='8ygc' size='340' side='right'caption='[[8ygc]], [[Resolution|resolution]] 4.03&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8ygc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8YGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YGC 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]] 4.03&#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=8ygc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ygc OCA], [https://pdbe.org/8ygc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ygc RCSB], [https://www.ebi.ac.uk/pdbsum/8ygc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ygc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/D4G637_BACNB D4G637_BACNB]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The NADase activity of the defense-associated sirtuins (DSRs) is activated by the phage tail tube protein (TTP). Herein, we report cryo-EM structures of a free-state Bacillus subtilis DSR2 tetramer and a fragment of the tetramer, a phage SPR tail tube, and two DSR2-TTP complexes. DSR2 contains an N-terminal SIR2 domain, a middle domain (MID) and a C-terminal domain (CTD). The DSR2 CTD harbors the alpha-solenoid tandem-repeats like the HEAT-repeat proteins. DSR2 assembles into a tetramer with four SIR2 clustered at the center, and two intertwined MID-CTD chains flank the SIR2 core. SPR TTPs self-assemble into a tube-like complex. Upon DSR2 binding, the D1 domain of SPR TTP is captured between the HEAT-repeats domains of DSR2, which conflicts with TTPs self-assembly. Binding of TTPs induces conformational changes in DSR2 tetramer, resulting in increase of the NAD(+) pocket volume in SIR2, thus activates the NADase activity and leads to cellular NAD(+) depletion.
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Authors:
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Activation of the bacterial defense-associated sirtuin system.,Zhu K, Shang K, Wang L, Yu X, Hua L, Zhang W, Qin B, Wang J, Gao X, Zhu H, Cui S Commun Biol. 2025 Feb 24;8(1):297. doi: 10.1038/s42003-025-07743-3. PMID:39994439<ref>PMID:39994439</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 8ygc" 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: Bacillus subtilis]]
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[[Category: Large Structures]]
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[[Category: Cui S]]
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[[Category: Gao X]]
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[[Category: Zhu H]]

Current revision

The Dimer Structure of DSR2-SPR

PDB ID 8ygc

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