1bt3
From Proteopedia
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CATECHOL OXIDASE FROM IPOMOEA BATATAS (SWEET POTATOES) IN THE NATIVE CU(II)-CU(II) STATE
Overview
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, ... [(full description)]
About this Structure
1BT3 is a [Single protein] structure of sequence from [Ipomoea batatas] with C2O as [ligand]. Active as [Catechol oxidase], with EC number [1.10.3.1]. Structure known Active Sites: CUA and CUB. Full crystallographic information is available from [OCA].
Reference
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
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