4YVU

Crystal structure of CotA native enzyme in the acid condition, PH5.6

4YVU の概要

• エントリーDOI: 10.2210/pdb4yvu/pdb
• 関連するPDBエントリー: 4YVN
• 分子名称: Spore coat protein A, COPPER (II) ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, spore coat protein a, laccase
• 由来する生物種: Bacillus subtilis (strain 168)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59105.79

構造登録者

Liu, Z.C.,Xie, T.,Wang, G.G. (登録日: 2015-03-20, 公開日: 2016-03-30, 最終更新日: 2024-11-06)

主引用文献

Liu, Z.,Xie, T.,Zhong, Q.,Wang, G.
Crystal structure of CotA laccase complexed with 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonate) at a novel binding site
Acta Crystallogr.,Sect.F, 72:328-335, 2016

PubMed Abstract: The CotA laccase from Bacillus subtilis is an abundant component of the spore outer coat and has been characterized as a typical laccase. The crystal structure of CotA complexed with 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonate) (ABTS) in a hole motif has been solved. The novel binding site was about 26 Å away from the T1 binding pocket. Comparison with known structures of other laccases revealed that the hole is a specific feature of CotA. The key residues Arg476 and Ser360 were directly bound to ABTS. Site-directed mutagenesis studies revealed that the residues Arg146, Arg429 and Arg476, which are located at the bottom of the novel binding site, are essential for the oxidation of ABTS and syringaldazine. Specially, a Thr480Phe variant was identified to be almost 3.5 times more specific for ABTS than for syringaldazine compared with the wild type. These results suggest this novel binding site for ABTS could be a potential target for protein engineering of CotA laccases.

PubMed: 27050268
DOI: 10.1107/S2053230X1600426X

実験手法

X-RAY DIFFRACTION (2.3 Å)