Unknown

Dataset Information

0

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.


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.

SUBMITTER: Nocek B 

PROVIDER: S-EPMC2678844 | BioStudies | 2007-01-01

REPOSITORIES: biostudies

Similar Datasets

2008-01-01 | S-EPMC2431047 | BioStudies
2016-01-01 | S-EPMC4807274 | BioStudies
1000-01-01 | S-EPMC2890747 | BioStudies
2009-01-01 | S-EPMC2704855 | BioStudies
2005-01-01 | S-EPMC2253363 | BioStudies
2007-01-01 | S-EPMC1885605 | BioStudies
2017-01-01 | S-EPMC5560556 | BioStudies
2016-01-01 | S-EPMC4901869 | BioStudies
1000-01-01 | S-EPMC6163384 | BioStudies
2019-01-01 | S-EPMC6450877 | BioStudies