6L9C

Neutron structure of copper amine oxidase from Arthrobacter glibiformis at pD 7.4

6L9C の概要

• エントリーDOI: 10.2210/pdb6l9c/pdb
• 分子名称: Phenylethylamine oxidase, COPPER (II) ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: copper amine oxidase, topaquinone, tpq, oxidoreductase
• 由来する生物種: Arthrobacter globiformis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 69080.37

構造登録者

Murakawa, T.,Kurihara, K.,Shoji, M.,Shibazaki, C.,Sunami, T.,Tamada, T.,Yano, N.,Yamada, T.,Kusaka, K.,Suzuki, M.,Shigeta, Y.,Kuroki, R.,Hayashi, H.,Yano, Y.,Tanizawa, K.,Adachi, M.,Okajima, T. (登録日: 2019-11-08, 公開日: 2020-04-29, 最終更新日: 2023-11-22)

主引用文献

Murakawa, T.,Kurihara, K.,Shoji, M.,Shibazaki, C.,Sunami, T.,Tamada, T.,Yano, N.,Yamada, T.,Kusaka, K.,Suzuki, M.,Shigeta, Y.,Kuroki, R.,Hayashi, H.,Yano, T.,Tanizawa, K.,Adachi, M.,Okajima, T.
Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing.
Proc.Natl.Acad.Sci.USA, 117:10818-10824, 2020

PubMed Abstract: Recent advances in neutron crystallographic studies have provided structural bases for quantum behaviors of protons observed in enzymatic reactions. Thus, we resolved the neutron crystal structure of a bacterial copper (Cu) amine oxidase (CAO), which contains a prosthetic Cu ion and a protein-derived redox cofactor, topa quinone (TPQ). We solved hitherto unknown structures of the active site, including a keto/enolate equilibrium of the cofactor with a nonplanar quinone ring, unusual proton sharing between the cofactor and the catalytic base, and metal-induced deprotonation of a histidine residue that coordinates to the Cu. Our findings show a refined active-site structure that gives detailed information on the protonation state of dissociable groups, such as the quinone cofactor, which are critical for catalytic reactions.

PubMed: 32371483
DOI: 10.1073/pnas.1922538117

実験手法

NEUTRON DIFFRACTION (1.72 Å)
X-RAY DIFFRACTION (1.14 Å)