ArticleJournal of molecular biology2007
Structure of an amide bond forming F(420):gamma-glutamyl ligase from Archaeoglobus fulgidus -- a member of a new family of non-ribosomal peptide synthases.
Article in Journal of molecular biology, 2007. 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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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Poly-γ-glutamylation of biomolecules.Nature communications · 2024Article
- Improved production of the non-native cofactor FScientific reports · 2021Article
- Cofactor F420: an expanded view of its distribution, biosynthesis and roles in bacteria and archaea.FEMS microbiology reviews · 2021Article
- Open Issues for Protein Function Assignment inGenes · 2021Article
- Article
- A revised biosynthetic pathway for the cofactor FNature communications · 2019Article
- Cofactor Tail Length Modulates Catalysis of Bacterial FFrontiers in microbiology · 2017Article
- The methanogenic redox cofactor FThe ISME journal · 2017Article
- Physiology, Biochemistry, and Applications of F420- and Fo-Dependent Redox Reactions.Microbiology and molecular biology reviews : MMBR · 2016Review
- Elongation of the Poly-γ-glutamate Tail of F420 Requires Both Domains of the F420:γ-Glutamyl Ligase (FbiB) of Mycobacterium tuberculosis.The Journal of biological chemistry · 2016Article
- The many roles of glutamate in metabolism.Journal of industrial microbiology & biotechnology · 2016Review
- Mutations in genes for the F420 biosynthetic pathway and a nitroreductase enzyme are the primary resistance determinants in spontaneous in vitro-selected PA-824-resistant mutants of Mycobacterium tuberculosis.Antimicrobial agents and chemotherapy · 2015Article
- Structural and functional characterization of microcin C resistance peptidase MccF from Bacillus anthracis.Journal of molecular biology · 2012Article
- Cloning, expression, purification, crystallization and preliminary X-ray studies of the C-terminal domain of Rv3262 (FbiB) from Mycobacterium tuberculosis.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- More than 200 genes required for methane formation from H₂ and CO₂ and energy conservation are present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus.Archaea (Vancouver, B.C.) · 2011Article
- Article
- Amidoligases with ATP-grasp, glutamine synthetase-like and acetyltransferase-like domains: synthesis of novel metabolites and peptide modifications of proteins.Molecular bioSystems · 2009Article
- Protein functional surfaces: global shape matching and local spatial alignments of ligand binding sites.BMC structural biology · 2008Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
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Abstract
F(420) is a flavin-like redox-active coenzyme commonly used by archaea and some eubacteria in a variety of biochemical reactions in methanogenesis, the formation of secondary metabolites, the degradation of nitroaromatic compounds, activation of nitroimidazofurans, and F(420)-dependent photolysis in DNA repair. Coenzyme F(420)-2 biosynthesis from 7,8-didemethyl-8-hydroxy-5-deazariboflavin (Fo) and lactaldehyde involves six enzymatic steps and five proteins (CofA, CofB, CofC, CofD, and CofE). CofE, a F(420)-0:gamma-glutamyl ligase, is responsible for the last two enzymatic steps; it catalyses the GTP-dependent addition of two L-glutamate residues to F(420)-0 to form F(420)-2. CofE is found in archaea, the aerobic actinomycetes, and cyanobacteria. Here, we report the first crystal structure of the apo-F(420)-0:gamma-glutamyl ligase (CofE-AF) from Archaeoglobus fulgidus and its complex with GDP at 2.5 A and 1.35 A resolution, respectively. The structure of CofE-AF reveals a novel protein fold with an intertwined, butterfly-like dimer formed by two-domain monomers. GDP and Mn(2+) are bound within the putative active site in a large groove at the dimer interface. We show that the enzyme adds a glutamate residue to both F(420)-0 and F(420)-1 in two distinct steps. CofE represents the first member of a new structural family of non-ribosomal peptide synthases.
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