ArticleThe Journal of biological chemistry2014
Mechanisms of allosteric activation and inhibition of the deoxyribonucleoside triphosphate triphosphohydrolase from Enterococcus faecalis.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Article
- Octameric dGTPase assemblies mediate broad anti-phage defense.Nature communications · 2026Article
- A deoxynucleoside triphosphate triphosphohydrolase promotes cell cycle progression inJournal of bacteriology · 2025Article
- The HD-Domain Metalloprotein Superfamily: An Apparent Common Protein Scaffold with Diverse Chemistries.Catalysts (Basel, Switzerland) · 2020Article
- 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
- A continuous spectrophotometric enzyme-coupled assay for deoxynucleoside triphosphate triphosphohydrolases.Analytical biochemistry · 2016Article
- Structure of Escherichia coli dGTP triphosphohydrolase: a hexameric enzyme with DNA effector molecules.The Journal of biological chemistry · 2015Article
- Structural basis of allosteric activation of sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) by nucleoside triphosphates.The Journal of biological chemistry · 2014Article
- Deoxyribonucleotides as genetic and metabolic regulators.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Review
- Allosteric regulation of the human and mouse deoxyribonucleotide triphosphohydrolase sterile α-motif/histidine-aspartate domain-containing protein 1 (SAMHD1).The Journal of biological chemistry · 2014Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
EF1143 from Enterococcus faecalis, a life-threatening pathogen that is resistant to common antibiotics, is a homo-tetrameric deoxyribonucleoside triphosphate (dNTP) triphosphohydrolase (dNTPase), converting dNTPs into the deoxyribonucleosides and triphosphate. The dNTPase activity of EF1143 is regulated by canonical dNTPs, which simultaneously act as substrates and activity modulators. Previous crystal structures of apo-EF1143 and the protein bound to both dGTP and dATP suggested allosteric regulation of its enzymatic activity by dGTP binding at four identical allosteric sites. However, whether and how other canonical dNTPs regulate the enzyme activity was not defined. Here, we present the crystal structure of EF1143 in complex with dGTP and dTTP. The new structure reveals that the tetrameric EF1143 contains four additional secondary allosteric sites adjacent to the previously identified dGTP-binding primary regulatory sites. Structural and enzyme kinetic studies indicate that dGTP binding to the first allosteric site, with nanomolar affinity, is a prerequisite for substrate docking and hydrolysis. Then, the presence of a particular dNTP in the second site either enhances or inhibits the dNTPase activity of EF1143. Our results provide the first mechanistic insight into dNTP-mediated regulation of dNTPase activity.
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