ArticleActa crystallographica. Section D, Biological crystallography2012
The structure of Enterococcus faecalis thymidylate synthase provides clues about folate bacterial metabolism.
Article in Acta crystallographica. Section D, Biological crystallography, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 36 citations in OpenAlex.
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- A Review on the Antimicrobial Activity of Schiff Bases: Data Collection and Recent Studies.Antibiotics (Basel, Switzerland) · 2022Review
- Multidrug Resistance (MDR): A Widespread Phenomenon in Pharmacological Therapies.Molecules (Basel, Switzerland) · 2022Review
- Bis-Thiourea Quaternary Ammonium Salts as Potential Agents against Bacterial Strains from Food and Environmental Matrices.Antibiotics (Basel, Switzerland) · 2021Article
- Benzothiazole-Containing Analogues of Triclocarban with Potent Antibacterial Activity.Antibiotics (Basel, Switzerland) · 2021Article
- The Different Facets of Triclocarban: A Review.Molecules (Basel, Switzerland) · 2021Review
- Searching for Small Molecules as Antibacterials: Non-Cytotoxic Diarylureas Analogues of Triclocarban.Antibiotics (Basel, Switzerland) · 2021Article
- Diarylureas: Repositioning from Antitumor to Antimicrobials or Multi-Target Agents against New Pandemics.Antibiotics (Basel, Switzerland) · 2021Review
- Targeting Methyltransferases in Human Pathogenic Bacteria: Insights into Thymidylate Synthase (TS) and Flavin-Dependent TS (FDTS).Molecules (Basel, Switzerland) · 2019Review
- Structural and Functional Characterization of the Human Thymidylate Synthase (hTS) Interface Variant R175C, New Perspectives for the Development of hTS Inhibitors.Molecules (Basel, Switzerland) · 2019Article
- Evidence of Destabilization of the Human Thymidylate Synthase (hTS) Dimeric Structure Induced by the Interface Mutation Q62R.Biomolecules · 2019Article
- Structural Comparison ofMolecules (Basel, Switzerland) · 2019Article
- A novel thymidylate synthase from thePeerJ · 2018Article
- Mg2+ binds to the surface of thymidylate synthase and affects hydride transfer at the interior active site.Journal of the American Chemical Society · 2013Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Drug resistance to therapeutic antibiotics poses a challenge to the identification of novel targets and drugs for the treatment of infectious diseases. Infections caused by Enterococcus faecalis are a major health problem. Thymidylate synthase (TS) from E. faecalis is a potential target for antibacterial therapy. The X-ray crystallographic structure of E. faecalis thymidylate synthase (EfTS), which was obtained as a native binary complex composed of EfTS and 5-formyltetrahydrofolate (5-FTHF), has been determined. The structure provides evidence that EfTS is a half-of-the-sites reactive enzyme, as 5-FTHF is bound to two of the four independent subunits present in the crystal asymmetric unit. 5-FTHF is a metabolite of the one-carbon transfer reaction catalysed by 5-formyltetrahydrofolate cyclo-ligase. Kinetic studies show that 5-FTHF is a weak inhibitor of EfTS, suggesting that the EfTS-5-FTHF complex may function as a source of folates and/or may regulate one-carbon metabolism. The structure represents the first example of endogenous 5-FTHF bound to a protein involved in folate metabolism.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.