1BT1

CATECHOL OXIDASE FROM IPOMOEA BATATAS (SWEET POTATOES) IN THE NATIVE CU(II)-CU(II) STATE

1BT1 の概要

• エントリーDOI: 10.2210/pdb1bt1/pdb
• 関連するPDBエントリー: 1BT2 1BT3 1BUG
• 分子名称: PROTEIN (CATECHOL OXIDASE), CU-O-CU LINKAGE (3 entities in total)
• 機能のキーワード: catechol oxidase, dicopper enzyme, ipomoea batatas, oxidoreductase
• 由来する生物種: Ipomoea batatas (sweet potato)
• 細胞内の位置: Plastid, chloroplast thylakoid lumen (By similarity): Q9ZP19
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77915.35

構造登録者

Klabunde, T.,Eicken, C.,Sacchettini, J.C.,Krebs, B. (登録日: 1998-09-02, 公開日: 1999-09-02, 最終更新日: 2024-10-30)

主引用文献

Klabunde, T.,Eicken, C.,Sacchettini, J.C.,Krebs, B.
Crystal structure of a plant catechol oxidase containing a dicopper center.
Nat.Struct.Biol., 5:1084-1090, 1998

PubMed Abstract: 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.

PubMed: 9846879
DOI: 10.1038/4193

実験手法

X-RAY DIFFRACTION (2.7 Å)