3SMA

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

3SMA の概要

• エントリーDOI: 10.2210/pdb3sma/pdb
• 分子名称: FrbF, ACETYL COENZYME *A (3 entities in total)
• 機能のキーワード: n-acetyl transferase, acetyl coa binding, transferase
• 由来する生物種: Streptomyces rubellomurinus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 129584.42

構造登録者

Bae, B.,Nair, S.K. (登録日: 2011-06-27, 公開日: 2011-08-24, 最終更新日: 2024-02-28)

主引用文献

Bae, B.,Cobb, R.E.,Desieno, M.A.,Zhao, H.,Nair, S.K.
New N-Acetyltransferase Fold in the Structure and Mechanism of the Phosphonate Biosynthetic Enzyme FrbF.
J.Biol.Chem., 286:36132-36141, 2011

PubMed 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.

PubMed: 21865168
DOI: 10.1074/jbc.M111.263533

実験手法

X-RAY DIFFRACTION (2 Å)