6I3J

Bilirubin oxidase from Myrothecium verrucaria in complex with ferricyanide

6I3J の概要

• エントリーDOI: 10.2210/pdb6i3j/pdb
• 関連するPDBエントリー: 6I3K 6I3L
• 分子名称: Bilirubin oxidase, CHLORIDE ION, R-1,2-PROPANEDIOL, ... (12 entities in total)
• 機能のキーワード: trp-his cross link, complex, oxidoreductase
• 由来する生物種: Albifimbria verrucaria
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 125991.64

構造登録者

Svecova, L.,Koval, T.,Skalova, T.,Kolenko, P.,Duskova, J.,Ostergaard, L.H.,Dohnalek, J. (登録日: 2018-11-06, 公開日: 2019-10-02, 最終更新日: 2024-10-16)

主引用文献

Koval, T.,Svecova, L.,Ostergaard, L.H.,Skalova, T.,Duskova, J.,Hasek, J.,Kolenko, P.,Fejfarova, K.,Stransky, J.,Trundova, M.,Dohnalek, J.
Trp-His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer.
Sci Rep, 9:13700-13700, 2019

PubMed Abstract: Unlike any protein studied so far, the active site of bilirubin oxidase from Myrothecium verrucaria contains a unique type of covalent link between tryptophan and histidine side chains. The role of this post-translational modification in substrate binding and oxidation is not sufficiently understood. Our structural and mutational studies provide evidence that this Trp396-His398 adduct modifies T1 copper coordination and is an important part of the substrate binding and oxidation site. The presence of the adduct is crucial for oxidation of substituted phenols and it substantially influences the rate of oxidation of bilirubin. Additionally, we bring the first structure of bilirubin oxidase in complex with one of its products, ferricyanide ion, interacting with the modified tryptophan side chain, Arg356 and the active site-forming loop 393-398. The results imply that structurally and chemically distinct types of substrates, including bilirubin, utilize the Trp-His adduct mainly for binding and to a smaller extent for electron transfer.

PubMed: 31548583
DOI: 10.1038/s41598-019-50105-3

実験手法

X-RAY DIFFRACTION (2.59 Å)