6FOQ

The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure.

6FOQ の概要

• エントリーDOI: 10.2210/pdb6foq/pdb
• 分子名称: Putative FAD-dependent oxygenase EncM, FLAVIN-ADENINE DINUCLEOTIDE, OXYGEN MOLECULE, ... (4 entities in total)
• 機能のキーワード: monooxygenase, flavin-n5-oxide, fad, encm, oxygenating species, oxygen binding, flavoprotein
• 由来する生物種: Streptomyces maritimus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 203695.68

構造登録者

Saleem-Batcha, R.,Teufel, R. (登録日: 2018-02-08, 公開日: 2018-05-02, 最終更新日: 2024-01-17)

主引用文献

Saleem-Batcha, R.,Stull, F.,Sanders, J.N.,Moore, B.S.,Palfey, B.A.,Houk, K.N.,Teufel, R.
Enzymatic control of dioxygen binding and functionalization of the flavin cofactor.
Proc. Natl. Acad. Sci. U.S.A., 115:4909-4914, 2018

PubMed Abstract: The reactions of enzymes and cofactors with gaseous molecules such as dioxygen (O) are challenging to study and remain among the most contentious subjects in biochemistry. To date, it is largely enigmatic how enzymes control and fine-tune their reactions with O, as exemplified by the ubiquitous flavin-dependent enzymes that commonly facilitate redox chemistry such as the oxygenation of organic substrates. Here we employ O-pressurized X-ray crystallography and quantum mechanical calculations to reveal how the precise positioning of O within a flavoenzyme's active site enables the regiospecific formation of a covalent flavin-oxygen adduct and oxygenating species (i.e., the flavin-N5-oxide) by mimicking a critical transition state. This study unambiguously demonstrates how enzymes may control the O functionalization of an organic cofactor as prerequisite for oxidative catalysis. Our work thus illustrates how O reactivity can be harnessed in an enzymatic environment and provides crucial knowledge for future rational design of O-reactive enzymes.

PubMed: 29686059
DOI: 10.1073/pnas.1801189115

実験手法

X-RAY DIFFRACTION (1.386 Å)