View source for 8ygp


==The tetramer Structure of DSR2-SPR with NAD==
<StructureSection load='8ygp' size='340' side='right'caption='[[8ygp]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ygp]] is a 8 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=8YGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YGP 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]] 4.4&#8491;</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=8ygp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ygp OCA], [https://pdbe.org/8ygp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ygp RCSB], [https://www.ebi.ac.uk/pdbsum/8ygp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ygp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D4G637_BACNB D4G637_BACNB] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ygp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Cui S]]
[[Category: Gao X]]
[[Category: Zhu H]]