ArticleThe Journal of biological chemistry2015
Crystal structure of DNA cytidine deaminase ABOBEC3G catalytic deamination domain suggests a binding mode of full-length enzyme to single-stranded DNA.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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39 citing papers in PubMed, 55 citations in OpenAlex.
- NMR in the Age of Modern Biomedical Research and Drug Discovery.Journal of molecular biology · 2025Review
- Article
- Direct inhibition of human APOBEC3 deaminases by HIV-1 Vif independent of the proteolysis pathway.Biophysical journal · 2024Article
- Two different kinds of interaction modes of deaminase APOBEC3A with single-stranded DNA in solution detected by nuclear magnetic resonance.Protein science : a publication of the Protein Society · 2022Article
- Review
- Characterization of an A3G-VifMolecular & cellular proteomics : MCP · 2021Article
- The Role of APOBECs in Viral Replication.Microorganisms · 2020Review
- Crystal Structure of a Soluble APOBEC3G Variant Suggests ssDNA to Bind in a Channel that Extends between the Two Domains.Journal of molecular biology · 2020Article
- Review
- Computational Investigation of APOBEC3H Substrate Orientation and Selectivity.The journal of physical chemistry. B · 2020Article
- Mechanism for APOBEC3G catalytic exclusion of RNA and non-substrate DNA.Nucleic acids research · 2019Article
- Structural Analysis of the Active Site and DNA Binding of Human Cytidine Deaminase APOBEC3B.Journal of chemical theory and computation · 2019Article
- Insight into dynamics of APOBEC3G protein in complexes with DNA assessed by high speed AFM.Nanoscale advances · 2019Article
- Modeling the Embrace of a Mutator: APOBEC Selection of Nucleic Acid Ligands.Trends in biochemical sciences · 2018Review
- Crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA.Nature communications · 2018Article
- ICBS 2017 in Shanghai-Illuminating Life with Chemical Innovation.ACS chemical biology · 2018Article
- Molecular Interactions of a DNA Modifying Enzyme APOBEC3F Catalytic Domain with a Single-Stranded DNA.Journal of molecular biology · 2018Article
- Insights into DNA substrate selection by APOBEC3G from structural, biochemical, and functional studies.PloS one · 2018Article
- Moloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G through interference with the Vif-mediated ubiquitin-proteasome pathway.Retrovirology · 2017Article
- Hydrogen bonds are a primary driving force for de novo protein folding.Acta crystallographica. Section D, Structural biology · 2017Article
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Authors and funding
9 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
APOBEC3G (A3G) is a DNA cytidine deaminase (CD) that demonstrates antiviral activity against human immunodeficiency virus 1 (HIV-1) and other pathogenic virus. It has an inactive N-terminal CD1 virus infectivity factor (Vif) protein binding domain (A3G-CD1) and an actively catalytic C-terminal CD2 deamination domain (A3G-CD2). Although many studies on the structure of A3G-CD2 and enzymatic properties of full-length A3G have been reported, the mechanism of how A3G interacts with HIV-1 single-stranded DNA (ssDNA) is still not well characterized. Here, we reported a crystal structure of a novel A3G-CD2 head-to-tail dimer (in which the N terminus of the monomer H (head) interacts with the C terminus of monomer T (tail)), where a continuous DNA binding groove was observed. By constructing the A3G-CD1 structural model, we found that its overall fold was almost identical to that of A3G-CD2. We mutated the residues located in or along the groove in monomer H and the residues in A3G-CD1 that correspond to those seated in or along the groove in monomer T. Then, by performing enzymatic assays, we confirmed the reported key elements and the residues in A3G necessary to the catalytic deamination. Moreover, we identified more than 10 residues in A3G essential to DNA binding and deamination reaction. Therefore, this dimer structure may represent a structural model of full-length A3G, which indicates a possible binding mode of A3G to HIV-1 ssDNA.
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