9B9M

Crystal structure of iron-bound FlcD from Pseudomonas aeruginosa

9B9M の概要

• エントリーDOI: 10.2210/pdb9b9m/pdb
• 分子名称: Pyrroloquinoline quinone (Coenzyme PQQ) biosynthesis protein C, FE (II) ION (3 entities in total)
• 機能のキーワード: mono-iron dioxygenase, oxidoreductase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 161184.36

構造登録者

Walker, M.E.,Grove, T.L.,Li, B.,Redinbo, M.R. (登録日: 2024-04-02, 公開日: 2024-07-31, 最終更新日: 2024-09-18)

主引用文献

Simke, W.C.,Walker, M.E.,Calderone, L.A.,Putz, A.T.,Patteson, J.B.,Vitro, C.N.,Zizola, C.F.,Redinbo, M.R.,Pandelia, M.E.,Grove, T.L.,Li, B.
Structural Basis for Methine Excision by a Heme Oxygenase-like Enzyme.
Acs Cent.Sci., 10:1524-1536, 2024

PubMed Abstract: Heme oxygenase-like domain-containing oxidases (HDOs) are a rapidly expanding enzyme family that typically use dinuclear metal cofactors instead of heme. FlcD, an HDO from the opportunistic pathogen , catalyzes the excision of an oxime carbon in the biosynthesis of the copper-containing antibiotic fluopsin C. We show that FlcD is a dioxygenase that catalyzes a four-electron oxidation. Crystal structures of FlcD reveal a mononuclear iron in the active site, which is coordinated by two histidines, one glutamate, and the oxime of the substrate. Enzyme activity, Mössbauer spectroscopy, and electron paramagnetic resonance spectroscopy analyses support the usage of a mononuclear iron cofactor. This cofactor resembles that of mononuclear non-heme iron-dependent enzymes and breaks the paradigm of dinuclear HDO cofactors. This study begins to illuminate the catalytic mechanism of methine excision and indicates convergent evolution of different lineages of mononuclear iron-dependent enzymes.

PubMed: 39220707
DOI: 10.1021/acscentsci.4c00015

実験手法

X-RAY DIFFRACTION (2.07 Å)