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http://purl.uniprot.org/citations/17669425http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17669425http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17669425http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/17669425http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2007.06.063"xsd:string
http://purl.uniprot.org/citations/17669425http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2007.06.063"xsd:string
http://purl.uniprot.org/citations/17669425http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2007.06.063"xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Edwards A."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Edwards A."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Evdokimova E."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Evdokimova E."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Joachimiak A."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Joachimiak A."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Kudritska M."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Kudritska M."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Nocek B."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Nocek B."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Proudfoot M."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Proudfoot M."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Savchenko A."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Savchenko A."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"White R.H."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"White R.H."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Yakunin A.F."xsd:string
http://purl.uniprot.org/citations/17669425http://purl.uniprot.org/core/author"Yakunin A.F."xsd:string