3sma | pdb_00003sma

A new N-acetyltransferase fold in the structure and mechanism of the phosphonate biosynthetic enzyme FrbF

spinqualitylabelsall models 3sma, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3sma is a 4 chain structure with sequence from "streptomyces_rubellomurinus"_iguchi_et_al._1980 "streptomyces rubellomurinus" iguchi et al. 1980. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACO Gene: frbF ("Streptomyces rubellomurinus" Iguchi et al. 1980) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The enzyme FrbF has attracted significant attention due to its role in 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. In spite of the established function as a bona fide N-acetyltransferase, FrbF shows no sequence similarity with any member of the GCN5-like N-acetyltransferase (GNAT) superfamily. Here, we present the 2.0 A resolution crystal structure of FrbF in complex with acetyl-CoA that demonstrates a unique architecture that is distinct from those of canonical GNAT-like acetyltransferases. We also utilize the co-crystal structure to guide structure-function studies that identify 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 provides a molecular framework towards the production of novel N-acyl derivatives of FR-900098. A new N-acetyltransferase fold in the structure and mechanism of the phosphonate biosynthetic enzyme FrbF.,Bae B, Cobb R, Desieno MA, Zhao H, Nair SK J Biol Chem. 2011 Aug 24. PMID:21865168 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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