pyrimidinones has been researched along with archaeosine* in 1 studies
1 other study(ies) available for pyrimidinones and archaeosine
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Crystal structure of the archaeosine synthase QueF-like-Insights into amidino transfer and tRNA recognition by the tunnel fold.
The tunneling-fold (T-fold) structural superfamily has emerged as a versatile protein scaffold of diverse catalytic activities. This is especially evident in the pathways to the 7-deazaguanosine modified nucleosides of tRNA queuosine and archaeosine. Four members of the T-fold superfamily have been confirmed in these pathways and here we report the crystal structure of a fifth enzyme; the recently discovered amidinotransferase QueF-Like (QueF-L), responsible for the final step in the biosynthesis of archaeosine in the D-loop of tRNA in a subset of Crenarchaeota. QueF-L catalyzes the conversion of the nitrile group of the 7-cyano-7-deazaguanine (preQ Topics: Amidinotransferases; Amino Acid Sequence; Archaeal Proteins; Catalytic Domain; Cloning, Molecular; Crystallography, X-Ray; Escherichia coli; Gene Expression; Guanosine; Molecular Docking Simulation; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Protein Multimerization; Protein Subunits; Pyrimidinones; Pyrobaculum; Pyrroles; Recombinant Proteins; RNA Processing, Post-Transcriptional; RNA, Archaeal; RNA, Transfer; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity | 2017 |