9n69

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Current revision (05:34, 23 April 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9n69 is ON HOLD until Paper Publication
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==Structure of the retron IA complex with HNH nuclease in the "down" orientation==
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<StructureSection load='9n69' size='340' side='right'caption='[[9n69]], [[Resolution|resolution]] 3.13&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9n69]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9N69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9N69 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]] 3.13&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=9n69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9n69 OCA], [https://pdbe.org/9n69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9n69 RCSB], [https://www.ebi.ac.uk/pdbsum/9n69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9n69 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0AAD2V6K7_ECOLX A0AAD2V6K7_ECOLX]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Reverse transcriptases (RTs) have well-established roles in the replication and spread of retroviruses and retrotransposons. However, recent evidence suggests that RTs have been conscripted by cells for diverse roles in antiviral defense. Here we determine structures of a type I-A retron, which explain how RNA, DNA, RT, HNH-nuclease and four molecules of an SMC-family ATPase assemble into a 364 kDa complex that provides phage defense. We show that phage-encoded nucleases trigger degradation of the retron-associated DNA, leading to disassembly of the retron and activation of the HNH nuclease. The HNH nuclease cleaves tRNA (Ser) , stalling protein synthesis and arresting viral replication. Taken together, these data reveal diverse and paradoxical roles for RTs in the perpetuation and elimination of genetic parasites.
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Authors:
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Structural basis of antiphage defense by an ATPase-associated reverse transcriptase.,George JT, Burman N, Wilkinson RA, de Silva S, McKelvey-Pham Q, Buyukyoruk M, Dale A, Landman H, Graham A, DeLuca SZ, Wiedenheft B bioRxiv [Preprint]. 2025 Mar 26:2025.03.26.645336. doi: , 10.1101/2025.03.26.645336. PMID:40196496<ref>PMID:40196496</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 9n69" 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: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Burman N]]
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[[Category: Thomas-George J]]
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[[Category: Wiedenheft B]]
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[[Category: Wilkinson R]]

Current revision

Structure of the retron IA complex with HNH nuclease in the "down" orientation

PDB ID 9n69

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