8tvc

Crystal structure of rA3G-ssDNA-AA

spinqualitylabelsall models 8tvc, resolution 1.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8tvc is a 2 chain structure with sequence from Macaca mulatta and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.93Å Ligands: PO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function M1GSK9_MACMU Publication Abstract from PubMed APOBEC3G, part of the AID/APOBEC cytidine deaminase family, is crucial for antiviral immunity. It has two zinc-coordinated cytidine-deaminase domains. The non-catalytic N-terminal domain strongly binds to nucleic acids, whereas the C-terminal domain catalyzes C-to-U editing in single-stranded DNA. The interplay between the two domains is not fully understood. Here, we show that DNA editing function of rhesus macaque APOBEC3G on linear and hairpin loop DNA is enhanced by AA or GA dinucleotide motifs present downstream in the 3'-direction of the target-C editing sites. The effective distance between AA/GA and the target-C sites is contingent on the local DNA secondary structure. We present two co-crystal structures of rhesus macaque APOBEC3G bound to ssDNA containing AA and GA, revealing the contribution of the non-catalytic domain in capturing AA/GA DNA. Our findings elucidate the molecular mechanism of APOBEC3G's cooperative function, which is critical for its antiviral role and its contribution to mutations in cancer genomes. Molecular mechanism for regulating APOBEC3G DNA editing function by the non-catalytic domain.,Yang H, Pacheco J, Kim K, Bokani A, Ito F, Ebrahimi D, Chen XS Nat Commun. 2024 Oct 10;15(1):8773. doi: 10.1038/s41467-024-52671-1. PMID:39389938 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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