ArticleProteins2017
Crystal structure of the archaeosine synthase QueF-like-Insights into amidino transfer and tRNA recognition by the tunnel fold.
Article in Proteins, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Biosynthesis and function of 7-deazaguanine derivatives in bacteria and phages.Microbiology and molecular biology reviews : MMBR · 2024Review
- Four additional natural 7-deazaguanine derivatives in phages and how to make them.Nucleic acids research · 2023Article
- Identification of a radical SAM enzyme involved in the synthesis of archaeosine.Nature chemical biology · 2019Article
- 7-Deazaguanine modifications protect phage DNA from host restriction systems.Nature communications · 2019Article
- Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA.Microorganisms · 2018Review
- Deazaguanine derivatives, examples of crosstalk between RNA and DNA modification pathways.RNA biology · 2017Review
- QueF-Like, a Non-Homologous Archaeosine Synthase from the Crenarchaeota.Biomolecules · 2017Article
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Authors and funding
6 authors.
Funding
Abstract
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
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