1W8E

3D structure of CotA incubated with hydrogen peroxide

1W8E の概要

• エントリーDOI: 10.2210/pdb1w8e/pdb
• 関連するPDBエントリー: 1GSK 1HKP 1HKZ 1HL0 1HL1 1OF0 1OGR 1UVW 1W6L 1W6W 2BHF
• 分子名称: SPORE COAT PROTEIN A, COPPER (II) ION, PEROXIDE ION, ... (5 entities in total)
• 機能のキーワード: multicopper-oxidase, laccase, oxygen reduction, oxidase
• 由来する生物種: BACILLUS SUBTILIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59137.25

構造登録者

Bento, I.,Martins, L.O.,Lopes, G.G.,Carrondo, M.A.,Lindley, P.F. (登録日: 2004-09-21, 公開日: 2005-10-26, 最終更新日: 2024-10-16)

主引用文献

Bento, I.,Martins, L.O.,Lopes, G.G.,Carrondo, M.A.,Lindley, P.F.
Dioxygen Reduction by Multi-Copper Oxidases; a Structural Perspective.
Dalton Trans., 7:3507-, 2005

PubMed Abstract: The multi-copper oxidases oxidise substrate molecules by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear centre. Dioxygen binds to the trinuclear centre and, following the transfer of four electrons, is reduced to two molecules of water. The precise mechanism of this reduction has been unclear, but recent X-ray structural studies using the CotA endospore coat protein from Bacillus subtilis have given further insights into the principal stages. It is proposed that the mechanism involves binding of the dioxygen into the trinuclear centre so that it is sited approximately symmetrically between the two type 3 copper ions with one oxygen atom close to the type 2 copper ion. Further stages involve the formation of a peroxide intermediate and following the splitting of this intermediate, the migration of the hydroxide moieties towards the solvent exit channel. The migration steps are likely to involve a movement of the type 2 copper ion and its environment. Details of a putative mechanism are described herein based both on structures already reported in the literature and on structures of the CotA protein in the oxidised and reduced states and with the addition of peroxide and the inhibitor, azide.

PubMed: 16234932
DOI: 10.1039/B504806K

実験手法

X-RAY DIFFRACTION (2.2 Å)