4tlf | pdb_00004tlf

Crystal structure of Thiol dioxygenase from Pseudomonas aeruginosa

spinqualitylabelsall models 4tlf, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4tlf is a 4 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.137Å Ligands: FE2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 3MDO_PSEAE Thiol dioxygenase that catalyzes the dioxygenation of 3-mercaptopropionate (3-MPA) to 3-sulfinopropionate (3-SPA). To a lesser extent (40-fold lower efficiency), is also able to oxidize cysteine to cysteine sulfinate (CSA). Cannot use N-acetyl-L-cysteine, homocysteine, and cysteamine as substrates. The physiological role of this enzyme is unclear. Publication Abstract from PubMed Thiol dioxygenation is the initial oxidation step that commits a thiol to important catabolic or biosynthetic pathways. The reaction is catalyzed by a family of specific non-heme mononuclear-iron proteins each of which is reported to react efficiently with only one substrate. This family of enzymes includes cysteine dioxygenase, cysteamine dioxygenase, mercaptosuccinate dioxygenase and 3-mercaptopropionate dioxygenase. Using sequence alignment to infer cysteine dioxygenase activity, a cysteine dioxygenase homologue from Pseudomonas aeruginosa (p3MDO) has been identified. Mass spectrometry of P. aeruginosa under standard growth conditions showed p3MDO is expressed in low levels suggesting that this metabolic pathway is available to the organism. Purified recombinant p3MDO is able to oxidize both cysteine and 3-mercaptopropionic acid (3-MPA) in vitro, with a marked preference for 3-MPA. We therefore describe this enzyme as a 3-mercaptopropionate dioxygenase. Mossbauer spectroscopy suggests that substrate binding to the ferrous iron is through the thiol but indicates each substrate could adopt different coordination geometries. Crystallographic comparison with mammalian cysteine dioxygenase shows that the overall active site geometry is conserved but suggests that the different substrate specificity can be related to replacement of an arginine by a glutamine in the active site. The Cysteine Dioxygenase Homologue from Pseudomonas aeruginosa is a 3-Mercaptopropionate Dioxygenase.,Tchesnokov EP, Fellner M, Siakkou E, Kleffmann T, Martin LW, Aloi S, Lamont IL, Wilbanks SM, Jameson GN J Biol Chem. 2015 Aug 13. pii: jbc.M114.635672. PMID:26272617 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dioxygenase 3D structures

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