1bt2

CATECHOL OXIDASE FROM IPOMOEA BATATAS (SWEET POTATOES) IN THE REDUCED CU(I)-CU(I) STATE

spinqualitylabelsall models 1bt2, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1bt2 is a 2 chain structure with sequence from Ipomoea batatas. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: C2O Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PPO1_IPOBA Catalyzes the oxidation of mono- and o-diphenols to o-diquinones. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Catechol oxidases are ubiquitous plant enzymes containing a dinuclear copper center. In the wound-response mechanism of the plant they catalyze the oxidation of a broad range of ortho-diphenols to the corresponding o-quinones coupled with the reduction of oxygen to water. The crystal structures of the enzyme from sweet potato in the resting dicupric Cu(II)-Cu(II) state, the reduced dicuprous Cu(I)-Cu(I) form, and in complex with the inhibitor phenylthiourea were analyzed. The catalytic copper center is accommodated in a central four-helix-bundle located in a hydrophobic pocket close to the surface. Both metal binding sites are composed of three histidine ligands. His 109, ligated to the CuA site, is covalently linked to Cys 92 by an unusual thioether bond. Based on biochemical, spectroscopic and the presented structural data, a catalytical mechanism is proposed in which one of the oxygen atoms of the diphenolic substrate binds to CuB of the oxygenated enzyme. Crystal structure of a plant catechol oxidase containing a dicopper center.,Klabunde T, Eicken C, Sacchettini JC, Krebs B Nat Struct Biol. 1998 Dec;5(12):1084-90. PMID:9846879 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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