ArticleThe Journal of biological chemistry2012
Structural basis of biological nitrile reduction.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 32 citations in OpenAlex.
- tRNA Modification Landscapes in Streptococci: Shared Losses and Clade-Specific Adaptations.bioRxiv : the preprint server for biology · 2025Article
- Biosynthesis and function of 7-deazaguanine derivatives in bacteria and phages.Microbiology and molecular biology reviews : MMBR · 2024Review
- Article
- Unexpected NADPH Hydratase Activity in the Nitrile Reductase QueF from Escherichia coli.Chembiochem : a European journal of chemical biology · 2020Article
- Crystal Structure of the Human tRNA Guanine Transglycosylase Catalytic Subunit QTRT1.Biomolecules · 2018Article
- Evidence of a sequestered imine intermediate during reduction of nitrile to amine by the nitrile reductase QueF fromThe Journal of biological chemistry · 2018Article
- To what extent do structural changes in catalytic metal sites affect enzyme function?Journal of inorganic biochemistry · 2018Article
- 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
- Protection of the Queuosine Biosynthesis Enzyme QueF from Irreversible Oxidation by a Conserved Intramolecular Disulfide.Biomolecules · 2017Article
- Crystal structure of the archaeosine synthase QueF-like-Insights into amidino transfer and tRNA recognition by the tunnel fold.Proteins · 2017Article
- Kinetic Analysis and Probing with Substrate Analogues of the Reaction Pathway of the Nitrile Reductase QueF from Escherichia coli.The Journal of biological chemistry · 2016Article
- Article
- Molecular modeling of the reaction pathway and hydride transfer reactions of HMG-CoA reductase.Biochemistry · 2012Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
The enzyme QueF catalyzes the reduction of the nitrile group of 7-cyano-7-deazaguanine (preQ(0)) to 7-aminomethyl-7-deazaguanine (preQ(1)), the only nitrile reduction reaction known in biology. We describe here two crystal structures of Bacillus subtilis QueF, one of the wild-type enzyme in complex with the substrate preQ(0), trapped as a covalent thioimide, a putative intermediate in the reaction, and the second of the C55A mutant in complex with the substrate preQ(0) bound noncovalently. The QueF enzyme forms an asymmetric tunnel-fold homodecamer of two head-to-head facing pentameric subunits, harboring 10 active sites at the intersubunit interfaces. In both structures, a preQ(0) molecule is bound at eight sites, and in the wild-type enzyme, it forms a thioimide covalent linkage to the catalytic residue Cys-55. Both structural and transient kinetic data show that preQ(0) binding, not thioimide formation, induces a large conformational change in and closure of the active site. Based on these data, we propose a mechanism for the activation of the Cys-55 nucleophile and subsequent hydride transfer.
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