9bf5
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Structure of V. cholerae DdmD in complex with ssDNA== | |
+ | <StructureSection load='9bf5' size='340' side='right'caption='[[9bf5]], [[Resolution|resolution]] 3.07Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[9bf5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BF5 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]] 3.07Å</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=9bf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9bf5 OCA], [https://pdbe.org/9bf5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9bf5 RCSB], [https://www.ebi.ac.uk/pdbsum/9bf5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9bf5 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/B9TSM3_VIBCL B9TSM3_VIBCL] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Horizontal gene transfer is a key driver of bacterial evolution, but it also presents severe risks to bacteria by introducing invasive mobile genetic elements. To counter these threats, bacteria have developed various defense systems, including prokaryotic Argonautes (pAgos) and the DNA defense module DdmDE system. Through biochemical analysis, structural determination, and in vivo plasmid clearance assays, we elucidate the assembly and activation mechanisms of DdmDE, which eliminates small, multicopy plasmids. We demonstrate that DdmE, a pAgo-like protein, acts as a catalytically inactive, DNA-guided, DNA-targeting defense module. In the presence of guide DNA, DdmE targets plasmids and recruits a dimeric DdmD, which contains nuclease and helicase domains. Upon binding to DNA substrates, DdmD transitions from an autoinhibited dimer to an active monomer, which then translocates along and cleaves the plasmids. Together, our findings reveal the intricate mechanisms underlying DdmDE-mediated plasmid clearance, offering fundamental insights into bacterial defense systems against plasmid invasions. | ||
- | + | DdmDE eliminates plasmid invasion by DNA-guided DNA targeting.,Yang XY, Shen Z, Wang C, Nakanishi K, Fu TM Cell. 2024 Aug 13:S0092-8674(24)00822-5. doi: 10.1016/j.cell.2024.07.028. PMID:39173632<ref>PMID:39173632</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 9bf5" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Vibrio cholerae]] | ||
+ | [[Category: Fu TM]] | ||
+ | [[Category: Shen ZF]] | ||
+ | [[Category: Yang XY]] |
Current revision
Structure of V. cholerae DdmD in complex with ssDNA
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