3S5W

Ornithine Hydroxylase (PvdA) from Pseudomonas aeruginosa

Summary for 3S5W

• Entry DOI: 10.2210/pdb3s5w/pdb
• Related: 3S61
• Descriptor: L-ornithine 5-monooxygenase, FLAVIN-ADENINE DINUCLEOTIDE, PHOSPHATE ION, ... (6 entities in total)
• Functional Keywords: class b flavin dependent n-hydroxylating monooxygenase, class b flavin dependent monooxygenase n-hydroxylating, monooxygenase, bacterial cytosol, oxidoreductase
• Biological source: Pseudomonas aeruginosa
• Cellular location: Cell inner membrane ; Peripheral membrane protein ; Cytoplasmic side : Q51548
• Total number of polymer chains: 2
• Total formula weight: 107061.47

Authors

Olucha, J.,Lamb, A.L. (deposition date: 2011-05-23, release date: 2011-07-13, Last modification date: 2024-04-03)

Primary citation

Olucha, J.,Meneely, K.M.,Chilton, A.S.,Lamb, A.L.
Two Structures of an N-Hydroxylating Flavoprotein Monooxygenase: ORNITHINE HYDROXYLASE FROM PSEUDOMONAS AERUGINOSA.
J.Biol.Chem., 286:31789-31798, 2011

PubMed Abstract: The ornithine hydroxylase from Pseudomonas aeruginosa (PvdA) catalyzes the FAD-dependent hydroxylation of the side chain amine of ornithine, which is subsequently formylated to generate the iron-chelating hydroxamates of the siderophore pyoverdin. PvdA belongs to the class B flavoprotein monooxygenases, which catalyze the oxidation of substrates using NADPH as the electron donor and molecular oxygen. Class B enzymes include the well studied flavin-containing monooxygenases and Baeyer-Villiger monooxygenases. The first two structures of a class B N-hydroxylating monooxygenase were determined with FAD in oxidized (1.9 Å resolution) and reduced (3.03 Å resolution) states. PvdA has the two expected Rossmann-like dinucleotide-binding domains for FAD and NADPH and also a substrate-binding domain, with the active site at the interface between the three domains. The structures have NADP(H) and (hydroxy)ornithine bound in a solvent-exposed active site, providing structural evidence for substrate and co-substrate specificity and the inability of PvdA to bind FAD tightly. Structural and biochemical evidence indicates that NADP(+) remains bound throughout the oxidative half-reaction, which is proposed to shelter the flavin intermediates from solvent and thereby prevent uncoupling of NADPH oxidation from hydroxylated product formation.

PubMed: 21757711
DOI: 10.1074/jbc.M111.265876

Experimental method

X-RAY DIFFRACTION (1.9 Å)