9n6b | pdb_00009n6b

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

spinqualitylabelsall models 9n6b, resolution 3.09Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9n6b is a 8 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.09Å Ligands: ATP, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0AAD2V6K7_ECOLX Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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