4A67

Mutations in the neighbourhood of CotA-laccase trinuclear site: D116E mutant

4A67 の概要

• エントリーDOI: 10.2210/pdb4a67/pdb
• 関連するPDBエントリー: 1GSK 1OF0 1UVW 1W6L 1W6W 1W8E 2BHF 2X87 2X88 4A66 4A68
• 分子名称: SPORE COAT PROTEIN A, COPPER (II) ION, PEROXIDE ION, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, multi-copper oxidase, oxidoreductase activity, trinuclear cluster, dioxygen reduction
• 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: 58891.00

構造登録者

Silva, C.S.,Lindley, P.F.,Bento, I. (登録日: 2011-10-31, 公開日: 2012-01-25, 最終更新日: 2023-12-20)

主引用文献

Silva, C.S.,Damas, J.M.,Chen, Z.,Brissos, V.,Martins, L.O.,Soares, C.M.,Lindley, P.F.,Bento, I.
The Role of Asp116 in the Reductive Cleavage of Dioxygen to Water in Cota Laccase: Assistance During the Proton Transfer Mechanism
Acta Crystallogr.,Sect.D, 68:186-, 2012

PubMed Abstract: Multi-copper oxidases constitute a family of proteins that are capable of coupling the one-electron oxidation of four substrate equivalents to the four-electron reduction of dioxygen to two molecules of water. The main catalytic stages occurring during the process have already been identified, but several questions remain, including the nature of the protonation events that take place during the reductive cleavage of dioxygen to water. The presence of a structurally conserved acidic residue (Glu498 in CotA laccase from Bacillus subtilis) at the dioxygen-entrance channel has been reported to play a decisive role in the protonation mechanisms, channelling protons during the reduction process and stabilizing the site as a whole. A second acidic residue that is sequentially conserved in multi-copper oxidases and sited within the exit channel (Asp116 in CotA) has also been identified as being important in the protonation process. In this study, CotA laccase has been used as a model system to assess the role of Asp116 in the reduction process of dioxygen to water. The crystal structures of three distinct mutants, D116E, D116N and D116A, produced by site-saturation mutagenesis have been determined. In addition, theoretical calculations have provided further support for a role of this residue in the protonation events.

PubMed: 22281748
DOI: 10.1107/S0907444911054503

実験手法

X-RAY DIFFRACTION (2.1 Å)