ArticleThe Journal of biological chemistry2015
Structure of Escherichia coli dGTP triphosphohydrolase: a hexameric enzyme with DNA effector molecules.
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 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- Manipulation of the nucleotide pool in human, bacterial and plant immunity.Nature reviews. Immunology · 2026Review
- A deoxynucleoside triphosphate triphosphohydrolase promotes cell cycle progression inJournal of bacteriology · 2025Article
- Reaction Mechanism and Metal Selectivity of Human SAMHD1 Elucidated by QM/MM Calculations.ACS catalysis · 2025Article
- Bacterial origins of human cell-autonomous innate immune mechanisms.Nature reviews. Immunology · 2022Review
- Mechanism by which T7 bacteriophage protein Gp1.2 inhibitsProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Bacteria deplete deoxynucleotides to defend against bacteriophage infection.Nature microbiology · 2022Article
- First Characterization of aFrontiers in microbiology · 2021Article
- Structure of Ddi2, a highly inducible detoxifying metalloenzyme fromThe Journal of biological chemistry · 2019Article
- The crystal structure of dGTPase reveals the molecular basis of dGTP selectivity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Single-Stranded Nucleic Acids Bind to the Tetramer Interface of SAMHD1 and Prevent Formation of the Catalytic Homotetramer.Biochemistry · 2016Article
- A continuous spectrophotometric enzyme-coupled assay for deoxynucleoside triphosphate triphosphohydrolases.Analytical biochemistry · 2016Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
The Escherichia coli dgt gene encodes a dGTP triphosphohydrolase whose detailed role still remains to be determined. Deletion of dgt creates a mutator phenotype, indicating that the dGTPase has a fidelity role, possibly by affecting the cellular dNTP pool. In the present study, we have investigated the structure of the Dgt protein at 3.1-Å resolution. One of the obtained structures revealed a protein hexamer that contained two molecules of single-stranded DNA. The presence of DNA caused significant conformational changes in the enzyme, including in the catalytic site of the enzyme. Dgt preparations lacking DNA were able to bind single-stranded DNA with high affinity (Kd ∼ 50 nM). DNA binding positively affected the activity of the enzyme: dGTPase activity displayed sigmoidal (cooperative) behavior without DNA but hyperbolic (Michaelis-Menten) kinetics in its presence, consistent with a specific lowering of the apparent Km for dGTP. A mutant Dgt enzyme was also created containing residue changes in the DNA binding cleft. This mutant enzyme, whereas still active, was incapable of DNA binding and could no longer be stimulated by addition of DNA. We also created an E. coli strain containing the mutant dgt gene on the chromosome replacing the wild-type gene. The mutant also displayed a mutator phenotype. Our results provide insight into the allosteric regulation of the enzyme and support a physiologically important role of DNA binding.
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