ArticleThe Journal of biological chemistry2016
Elongation of the Poly-γ-glutamate Tail of F420 Requires Both Domains of the F420:γ-Glutamyl Ligase (FbiB) of Mycobacterium tuberculosis.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Flavin and deazaflavin biosynthesis in mycobacteria: relevance to physiology, implications for drug discovery, MR-1 antigenicity, and vaccine development.Frontiers in immunology · 2025Review
- Cyclodipeptide oxidase is an enzyme filament.Nature communications · 2024Article
- Poly-γ-glutamylation of biomolecules.Nature communications · 2024Article
- Deazaflavin metabolite produced by endosymbiotic bacteria controls fungal host reproduction.The ISME journal · 2024Article
- Identification ofInfection and drug resistance · 2024Review
- Diversification by CofC and Control by CofD Govern Biosynthesis and Evolution of Coenzyme FmBio · 2022Article
- Cofactor F420: an expanded view of its distribution, biosynthesis and roles in bacteria and archaea.FEMS microbiology reviews · 2021Article
- Redox Coenzyme FApplied and environmental microbiology · 2020Article
- Article
- Adduct Formation of Delamanid with NAD in Mycobacteria.Antimicrobial agents and chemotherapy · 2020Article
- A revised biosynthetic pathway for the cofactor FNature communications · 2019Article
- Coenzyme FJournal of bacteriology · 2018Article
- Evolutionary and molecular foundations of multiple contemporary functions of the nitroreductase superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The methanogenic redox cofactor FThe ISME journal · 2017Article
- Cofactor Tail Length Modulates Catalysis of Bacterial FFrontiers in microbiology · 2017Article
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Authors and funding
6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Cofactor F420is an electron carrier with a major role in the oxidoreductive reactions ofMycobacterium tuberculosis, the causative agent of tuberculosis. A γ-glutamyl ligase catalyzes the final steps of the F420biosynthesis pathway by successive additions ofl-glutamate residues to F420-0, producing a poly-γ-glutamate tail. The enzyme responsible for this reaction in archaea (CofE) comprises a single domain and produces F420-2 as the major species. The homologousM. tuberculosisenzyme, FbiB, is a two-domain protein and produces F420with predominantly 5-7l-glutamate residues in the poly-γ-glutamate tail. The N-terminal domain of FbiB is homologous to CofE with an annotated γ-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Here we demonstrate that full-length FbiB adds multiplel-glutamate residues to F420-0in vitroto produce F420-5 after 24 h; communication between the two domains is critical for full γ-glutamyl ligase activity. We also present crystal structures of the C-terminal domain of FbiB in apo-, F420-0-, and FMN-bound states, displaying distinct sites for F420-0 and FMN ligands that partially overlap. Finally, we discuss the features of a full-length structural model produced by small angle x-ray scattering and its implications for the role of N- and C-terminal domains in catalysis.
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