5ZLL

Mutation in the trinuclear site of CotA-laccase: H493C mutant, PH 8.0

5ZLL の概要

• エントリーDOI: 10.2210/pdb5zll/pdb
• 関連するPDBエントリー: 5ZLK
• 分子名称: Spore coat protein A, COPPER (II) ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Bacillus subtilis subsp. subtilis str. 168
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59070.79

構造登録者

Xie, T.,Liu, Z.C.,Wang, G.G. (登録日: 2018-03-28, 公開日: 2018-05-16, 最終更新日: 2024-11-13)

主引用文献

Xie, T.,Liu, Z.,Wang, G.
Structural Insight into the Allosteric Coupling of Cu1 Site and Trinuclear Cu Cluster in CotA Laccase.
Chembiochem, 19:1502-1506, 2018

PubMed Abstract: In laccase, type 1 copper (Cu1) was connected to the trinuclear copper center (TNC) by the conserved Cys-His bridge. An allosteric coupling between the two redox sites has been reported; however, the molecular mechanism underlining the allosteric coupling is unknown. In this study, ligands of the two type 3 copper sites, including His491 and His493, in CotA were mutated to Cys or Ala. The crystal structures revealed that mutations at His491 and His493 caused rearrangement of the hydrogen-bond network and geometric distortion of the TNC, which severely impaired the activities of mutants H493A, H493C, and H491C. In addition, the change in TNC affected hydrogen bonds around Cys492 in the mutants and led to Cu1 being partially reduced. These results not only decipher the mechanism of allosteric coupling between Cu1 and TNC in laccase, but also pave the way for laccase protein engineering.

PubMed: 29722464
DOI: 10.1002/cbic.201800236

実験手法

X-RAY DIFFRACTION (2.6 Å)