6OMP

Crystal structure of apo PtmU3

6OMP の概要

• エントリーDOI: 10.2210/pdb6omp/pdb
• 分子名称: PtmU3, ACETATE ION, MANGANESE (II) ION, ... (4 entities in total)
• 機能のキーワード: tim-barrel, oxidoreductase
• 由来する生物種: Streptomyces platensis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79800.40

構造登録者

Liu, Y.C.,Dong, L.B.,Shen, B. (登録日: 2019-04-19, 公開日: 2019-07-24, 最終更新日: 2024-03-13)

主引用文献

Dong, L.B.,Liu, Y.C.,Cepeda, A.J.,Kalkreuter, E.,Deng, M.R.,Rudolf, J.D.,Chang, C.,Joachimiak, A.,Phillips Jr., G.N.,Shen, B.
Characterization and Crystal Structure of a Nonheme Diiron Monooxygenase Involved in Platensimycin and Platencin Biosynthesis.
J.Am.Chem.Soc., 141:12406-12412, 2019

PubMed Abstract: Nonheme diiron monooxygenases make up a rapidly growing family of oxygenases that are rarely identified in secondary metabolism. Herein, we report the in vivo, in vitro, and structural characterizations of a nonheme diiron monooxygenase, PtmU3, that installs a C-5 β-hydroxyl group in the unified biosynthesis of platensimycin and platencin, two highly functionalized diterpenoids that act as potent and selective inhibitors of bacterial and mammalian fatty acid synthases. This hydroxylation sets the stage for the subsequent A-ring cleavage step key to the unique diterpene-derived scaffolds of platensimycin and platencin. PtmU3 adopts an unprecedented triosephosphate isomerase (TIM) barrel structural fold for this class of enzymes and possesses a noncanonical diiron active site architecture with a saturated six-coordinate iron center lacking a μ-oxo bridge. This study reveals the first member of a previously unidentified superfamily of TIM-barrel-fold enzymes for metal-dependent dioxygen activation, with the majority predicted to act on CoA-linked substrates, thus expanding our knowledge of nature's repertoire of nonheme diiron monooxygenases and TIM-barrel-fold enzymes.

PubMed: 31291107
DOI: 10.1021/jacs.9b06183

実験手法

X-RAY DIFFRACTION (1.7 Å)