View source for 8xfe


==Cryo-EM structure of defence-associated sirtuin 2 (DSR2) H171A protein in complex with DSR anti-defence 1(DSAD1)==
<StructureSection load='8xfe' size='340' side='right'caption='[[8xfe]], [[Resolution|resolution]] 2.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8xfe]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._DSM_5850 Bacillus sp. DSM 5850] and [https://en.wikipedia.org/wiki/Phage_#D Phage #D]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XFE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XFE 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]] 2.98&#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=8xfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xfe OCA], [https://pdbe.org/8xfe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xfe RCSB], [https://www.ebi.ac.uk/pdbsum/8xfe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xfe ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
As a sirtuin (SIR2) family protein, defense-associated sirtuin2 (DSR2) has been demonstrated to participate in bacterial anti-phage resistance via depleting nicotinamide adenine dinucleotide (NAD(+)) of infected cells, which can be activated by tail tube protein (TTP) and inhibited by DSR anti-defense 1 (DSAD1) of diverse phages. However, the regulating mechanism remains elusive. Here, we determined the cryo-electron microscopy structure of apo DSR2, as well as the respective complex structures with TTP and DSAD1. Structural analyses and biochemical studies reveal that DSR2 forms a tetramer with a SIR2 central core and two distinct conformations. Monomeric TTP preferentially binds to the closed conformation of DSR2, inducing conformational distortions on SIR2 tetramer assembly to activate its NADase activity. DSAD1 combines with the open conformation of DSR2, directly or allosterically inhibiting TTP activation on DSR2 NAD(+) hydrolysis. Our findings decipher the detailed molecule mechanisms for DSR2 NADase activity regulation and lay a foundation for in-depth understanding of the DSR2 anti-phage defense system.

Structural insights into activation mechanisms on NADase of the bacterial DSR2 anti-phage defense system.,Zhang H, Li Y, Li L, Chen L, Zhu C, Sun L, Dong P, Jing D, Yang J, Fu L, Xiao F, Xia N, Li S, Zheng Q, Wu Y Sci Adv. 2024 Aug 2;10(31):eadn5691. doi: 10.1126/sciadv.adn5691. Epub 2024 Jul , 31. PMID:39083599<ref>PMID:39083599</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8xfe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus sp. DSM 5850]]
[[Category: Large Structures]]
[[Category: Phage #D]]
[[Category: Li S]]
[[Category: Li Y]]
[[Category: Wu Y]]
[[Category: Zhang H]]
[[Category: Zheng Q]]