7OUC

Crystal structure of the flavoprotein monooxygenase GrhO5 from griseorhodin A biosynthesis

これはPDB形式変換不可エントリーです。

7OUC の概要

• エントリーDOI: 10.2210/pdb7ouc/pdb
• 分子名称: Putative FAD-dependent monooxygenase GrhO5, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: flavoprotein, monooxygenase, griseorhodin a biosynthesis, rubromycin biosynthesis
• 由来する生物種: Streptomyces sp. JP95
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56511.71

構造登録者

Saleem-Batcha, R.,Toplak, M.,Teufel, R. (登録日: 2021-06-11, 公開日: 2021-11-03, 最終更新日: 2024-01-31)

主引用文献

Toplak, M.,Saleem-Batcha, R.,Piel, J.,Teufel, R.
Catalytic Control of Spiroketal Formation in Rubromycin Polyketide Biosynthesis.
Angew.Chem.Int.Ed.Engl., 60:26960-26970, 2021

PubMed Abstract: The medically important bacterial aromatic polyketide natural products typically feature a planar, polycyclic core structure. An exception is found for the rubromycins, whose backbones are disrupted by a bisbenzannulated [5,6]-spiroketal pharmacophore that was recently shown to be assembled by flavin-dependent enzymes. In particular, a flavoprotein monooxygenase proved critical for the drastic oxidative rearrangement of a pentangular precursor and the installment of an intermediate [6,6]-spiroketal moiety. Here we provide structural and mechanistic insights into the control of catalysis by this spiroketal synthase, which fulfills several important functions as reductase, monooxygenase, and presumably oxidase. The enzyme hereby tightly controls the redox state of the substrate to counteract shunt product formation, while also steering the cleavage of three carbon-carbon bonds. Our work illustrates an exceptional strategy for the biosynthesis of stable chroman spiroketals.

PubMed: 34652045
DOI: 10.1002/anie.202109384

実験手法

X-RAY DIFFRACTION (1.75 Å)