ArticleThe Journal of biological chemistry2011
New N-acetyltransferase fold in the structure and mechanism of the phosphonate biosynthetic enzyme FrbF.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 11 citations in OpenAlex.
- Structural and molecular rationale for the diversification of resistance mediated by the Antibiotic_NAT family.Communications biology · 2022Article
- Classification and phylogeny for the annotation of novel eukaryotic GNAT acetyltransferases.PLoS computational biology · 2020Article
- A low-barrier hydrogen bond mediates antibiotic resistance in a noncanonical catalytic triad.Science advances · 2018Article
- Phosphonate biosynthesis and catabolism: a treasure trove of unusual enzymology.Current opinion in chemical biology · 2013Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The enzyme FrbF from Streptomyces rubellomurinus has attracted significant attention due to its role in the biosynthesis of the antimalarial phosphonate FR-900098. The enzyme catalyzes acetyl transfer onto the hydroxamate of the FR-900098 precursors cytidine 5'-monophosphate-3-aminopropylphosphonate and cytidine 5'-monophosphate-N-hydroxy-3-aminopropylphosphonate. Despite the established function as a bona fide N-acetyltransferase, FrbF shows no sequence similarity to any member of the GCN5-like N-acetyltransferase (GNAT) superfamily. Here, we present the 2.0 Å resolution crystal structure of FrbF in complex with acetyl-CoA, which demonstrates a unique architecture that is distinct from those of canonical GNAT-like acetyltransferases. We also utilized the co-crystal structure to guide structure-function studies that identified the roles of putative active site residues in the acetyltransferase mechanism. The combined biochemical and structural analyses of FrbF provide insights into this previously uncharacterized family of N-acetyltransferases and also provide a molecular framework toward the production of novel N-acyl derivatives of FR-900098.
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