3s61

Reduced Form of Ornithine Hydroxylase (PvdA) from Pseudomonas aeruginosa

spinqualitylabelsall models 3s61, resolution 3.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3s61 is a 2 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD, NDP, ORN Related: 3s5w Gene: PA2386, pvd-1, pvdA ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PVDA_PSEAE] Catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as pyoverdin. Pyoverdin is a hydroxamate siderophore composed of a 6,7-dihydroxyquinoline-containing fluorescent chromophore joined to the N-terminus of a partly cyclic octapeptide (D-Ser-L-Arg-D-Ser-L-N(5)-OH-Orn-L-Lys-L-N(5)-OH-Orn-L-Thr-L-Thr in strain PAO1). Specific for NADPH, which plays a role in stabilization of the C4a-hydroperoxyflavin intermediate. Publication Abstract from PubMed The ornithine hydroxylase from Pseudomonas aeruginosa (PvdA) catalyzes the FAD dependent hydroxylation of the sidechain 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 electron donor and molecular oxygen. Class B enzymes include the well-studied flavin-containing monooxygenases and Baeyer-Villiger monoogenases. The first two structures of a class B N-hydroxylating monooxygenase were determined with the FAD in oxidized (1.9 A resolution) and reduced states (3.03 A). PvdA has the two expected Rossman-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 indicate 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. Two structures of an N-hydroxylating flavoprotein monooxgenase: the ornithine hydroxylase from Pseudomonas aeruginosa.,Olucha J, Meneely KM, Chilton AS, Lamb AL J Biol Chem. 2011 Jul 13. PMID:21757711 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monooxygenase 3D structures

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