6NIE

BesD with Fe(II), chloride, and alpha-ketoglutarate

6NIE の概要

• エントリーDOI: 10.2210/pdb6nie/pdb
• 分子名称: BesD, lysine halogenase, LYSINE, FE (II) ION, ... (7 entities in total)
• 機能のキーワード: halogenase, biosynthetic protein
• 由来する生物種: Streptomyces cattleya (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 118870.31

構造登録者

Neugebauer, M.E.,Chang, M.C.Y. (登録日: 2018-12-27, 公開日: 2019-10-02, 最終更新日: 2024-03-13)

主引用文献

Neugebauer, M.E.,Sumida, K.H.,Pelton, J.G.,McMurry, J.L.,Marchand, J.A.,Chang, M.C.Y.
A family of radical halogenases for the engineering of amino-acid-based products.
Nat.Chem.Biol., 15:1009-1016, 2019

PubMed Abstract: The integration of synthetic and biological catalysis enables new approaches to the synthesis of small molecules by combining the high selectivity of enzymes with the reaction diversity offered by synthetic chemistry. While organohalogens are valued for their bioactivity and utility as synthetic building blocks, only a handful of enzymes that carry out the regioselective halogenation of unactivated [Formula: see text] bonds have previously been identified. In this context, we report the structural characterization of BesD, a recently discovered radical halogenase from the Fe/α-ketogluturate-dependent family that chlorinates the free amino acid lysine. We also identify and characterize additional halogenases that produce mono- and dichlorinated, as well as brominated and azidated, amino acids. The substrate selectivity of this new family of radical halogenases takes advantage of the central role of amino acids in metabolism and enables engineering of biosynthetic pathways to afford a wide variety of compound classes, including heterocycles, diamines, α-keto acids and peptides.

PubMed: 31548692
DOI: 10.1038/s41589-019-0355-x

実験手法

X-RAY DIFFRACTION (1.95 Å)