ArticleThe Journal of biological chemistry2011
Characterization of the deoxynucleotide triphosphate triphosphohydrolase (dNTPase) activity of the EF1143 protein from Enterococcus faecalis and crystal structure of the activator-substrate complex.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 41 citations in OpenAlex.
- Octameric dGTPase assemblies mediate broad anti-phage defense.Nature communications · 2026Article
- Article
- 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
- Mechanisms supporting aminoadenine-based viral DNA genomes.Cellular and molecular life sciences : CMLS · 2021Review
- The HD-Domain Metalloprotein Superfamily: An Apparent Common Protein Scaffold with Diverse Chemistries.Catalysts (Basel, Switzerland) · 2020Article
- The missing link: allostery and catalysis in the anti-viral protein SAMHD1.Biochemical Society transactions · 2019Review
- 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
- SAMHD1: Recurring roles in cell cycle, viral restriction, cancer, and innate immunity.Autoimmunity · 2018Review
- An HD domain phosphohydrolase active site tailored for oxetanocin-A biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- 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
- Purification, crystallization and preliminary X-ray analysis of a putative nucleotide phosphohydrolase, YpgQ, from Bacillus subtilis.Acta crystallographica. Section F, Structural biology communications · 2014Article
- 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
- GTP activator and dNTP substrates of HIV-1 restriction factor SAMHD1 generate a long-lived activated state.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Mechanisms of allosteric activation and inhibition of the deoxyribonucleoside triphosphate triphosphohydrolase from Enterococcus faecalis.The Journal of biological chemistry · 2014Article
- Contribution of oligomerization to the anti-HIV-1 properties of SAMHD1.Retrovirology · 2013Article
- Mechanism of allosteric activation of SAMHD1 by dGTP.Nature structural & molecular biology · 2013Article
- The deoxynucleotide triphosphohydrolase SAMHD1 is a major regulator of DNA precursor pools in mammalian cells.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
The EF1143 protein from Enterococcus faecalis is a distant homolog of deoxynucleotide triphosphate triphosphohydrolases (dNTPases) from Escherichia coli and Thermus thermophilus. These dNTPases are important components in the regulation of the dNTP pool in bacteria. Biochemical assays of the EF1143 dNTPase activity demonstrated nonspecific hydrolysis of all canonical dNTPs in the presence of Mn(2+). In contrast, with Mg(2+) hydrolysis required the presence of dGTP as an effector, activating the degradation of dATP and dCTP with dGTP also being consumed in the reaction with dATP. The crystal structure of EF1143 and dynamic light scattering measurements in solution revealed a tetrameric oligomer as the most probable biologically active unit. The tetramer contains four dGTP specific allosteric regulatory sites and four active sites. Examination of the active site with the dATP substrate suggests an in-line nucleophilic attack on the α-phosphate center as a possible mechanism of the hydrolysis and two highly conserved residues, His-129 and Glu-122, as an acid-base catalytic dyad. Structural differences between EF1143 apo and holo forms revealed mobility of the α3 helix that can regulate the size of the active site binding pocket and could be stabilized in the open conformation upon formation of the tetramer and dGTP effector binding.
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