ArticleThe Journal of biological chemistry2014
Streptococcus sanguinis class Ib ribonucleotide reductase: high activity with both iron and manganese cofactors and structural insights.
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 32 papers.
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Who cites it
32 citing papers in PubMed, 48 citations in OpenAlex.
- Kinetically Divergent Dimanganese-Tyrosyl Radical Cofactor Assembly in Listeria monocytogenes Class I Ribonucleotide Reductase.Biochemistry · 2026Article
- Phosphoester hydrolysis using a de novo designed protein: A combined experimental and computational study.Journal of inorganic biochemistry · 2026Article
- Review
- Article
- In Vitro and In Silico Studies of the Antimicrobial Activity of Prenylated Phenylpropanoids of Green Propolis and Their Derivatives against Oral Bacteria.Antibiotics (Basel, Switzerland) · 2024Article
- Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023Review
- Article
- Managing Manganese: The Role of Manganese Homeostasis in Streptococcal Pathogenesis.Frontiers in cell and developmental biology · 2022Review
- Ferritin-Like Proteins: A Conserved Core for a Myriad of Enzyme Complexes.Sub-cellular biochemistry · 2022Article
- Regulation and distinct physiological roles of manganese in bacteria.FEMS microbiology reviews · 2021Review
- Time-course analysis of Streptococcus sanguinis after manganese depletion reveals changes in glycolytic and nucleic acid metabolites.Metabolomics : Official journal of the Metabolomic Society · 2021Article
- Intracellular Metal Speciation inACS infectious diseases · 2020Article
- Ribonucleotide Reductases: Structure, Chemistry, and Metabolism Suggest New Therapeutic Targets.Annual review of biochemistry · 2020Review
- Subunit Interaction Dynamics of Class Ia Ribonucleotide Reductases: In Search of a Robust Assay.Biochemistry · 2020Article
- Manganese Depletion Leads to Multisystem Changes in the Transcriptome of the Opportunistic PathogenFrontiers in microbiology · 2020Article
- Murine Calprotectin Coordinates Mn(II) at a Hexahistidine Site with Ca(II)-Dependent Affinity.Inorganic chemistry · 2019Article
- Class Id ribonucleotide reductase utilizes a MnJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Convergent allostery in ribonucleotide reductase.Nature communications · 2019Article
- Genomic, Phenotypic, and Virulence Analysis ofInfection and immunity · 2019Article
- Metal-free class Ie ribonucleotide reductase from pathogens initiates catalysis with a tyrosine-derived dihydroxyphenylalanine radical.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Streptococcus sanguinis is a causative agent of infective endocarditis. Deletion of SsaB, a manganese transporter, drastically reduces S. sanguinis virulence. Many pathogenic organisms require class Ib ribonucleotide reductase (RNR) to catalyze the conversion of nucleotides to deoxynucleotides under aerobic conditions, and recent studies demonstrate that this enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(•)) cofactor in vivo. The proteins required for S. sanguinis ribonucleotide reduction (NrdE and NrdF, α and β subunits of RNR; NrdH and TrxR, a glutaredoxin-like thioredoxin and a thioredoxin reductase; and NrdI, a flavodoxin essential for assembly of the RNR metallo-cofactor) have been identified and characterized. Apo-NrdF with Fe(II) and O2 can self-assemble a diferric-tyrosyl radical (Fe(III)2-Y(•)) cofactor (1.2 Y(•)/β2) and with the help of NrdI can assemble a Mn(III)2-Y(•) cofactor (0.9 Y(•)/β2). The activity of RNR with its endogenous reductants, NrdH and TrxR, is 5,000 and 1,500 units/mg for the Mn- and Fe-NrdFs (Fe-loaded NrdF), respectively. X-ray structures of S. sanguinis NrdIox and Mn(II)2-NrdF are reported and provide a possible rationale for the weak affinity (2.9 μM) between them. These streptococcal proteins form a structurally distinct subclass relative to other Ib proteins with unique features likely important in cluster assembly, including a long and negatively charged loop near the NrdI flavin and a bulky residue (Thr) at a constriction in the oxidant channel to the NrdI interface. These studies set the stage for identifying the active form of S. sanguinis class Ib RNR in an animal model for infective endocarditis and establishing whether the manganese requirement for pathogenesis is associated with RNR.
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