8W1Q

Aerobic crystal structure of iron-bound FlcD from Pseudomonas aeruginosa

Summary for 8W1Q

• Entry DOI: 10.2210/pdb8w1q/pdb
• Descriptor: Pyrroloquinoline quinone (Coenzyme PQQ) biosynthesis protein C, FE (II) ION, POTASSIUM ION, ... (6 entities in total)
• Functional Keywords: mono-iron dioxygenase, oxidoreductase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 80786.78

Authors

Walker, M.E.,Grove, T.L.,Li, B.,Redinbo, M.R. (deposition date: 2024-02-17, release date: 2024-07-31, Last modification date: 2024-09-18)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.56 Å)