2XLL

The crystal structure of bilirubin oxidase from Myrothecium verrucaria

2XLL の概要

• エントリーDOI: 10.2210/pdb2xll/pdb
• 分子名称: BILIRUBIN OXIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, COPPER (II) ION, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, blue multicopper oxidase, laccase, ascomycete, dioxygen reduction, heme catabolism, glycoprotein, protein film voltammetry
• 由来する生物種: MYROTHECIUM VERRUCARIA
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 244450.70

構造登録者

McNamara, T.P.,Lowe, E.D.,Cracknell, J.A.,Blanford, C.F. (登録日: 2010-07-21, 公開日: 2011-04-20, 最終更新日: 2024-11-06)

主引用文献

Cracknell, J.A.,Mcnamara, T.P.,Lowe, E.D.,Blanford, C.F.
Bilirubin Oxidase from Myrothecium Verrucaria: X- Ray Determination of the Complete Crystal Structure and a Rational Surface Modification for Enhanced Electrocatalytic O(2) Reduction.
Dalton Trans, 40:6668-, 2011

PubMed Abstract: The blue multi-copper oxidase bilirubin oxidase (BOx) from the ascomycete plant pathogen Myrothecium verrucaria (Mv) efficiently catalyses the oxidation of bilirubin to biliverdin, with the concomitant reduction of O(2) to water, a reaction of considerable interest for low-temperature bio-fuel cell applications. We have solved the complete X-ray determined structure of Mv BOx at 2.4 Å resolution, using molecular replacement with the Spore Coat Protein A (CotA) enzyme from Bacillus subtilis (PDB code 1GSK) as a template. The structure reveals an unusual environment around the blue type 1 copper (T1 Cu) that includes two non-coordinating hydrophilic amino acids, asparagine and threonine. The presence of a long, narrow and hydrophilic pocket near the T1 Cu suggests that structure of the substrate-binding site is dynamically determined in vivo. We show that the interaction between the binding pocket of Mv BOx and its highly conjugated natural organic substrate, bilirubin, can be used to stabilise the enzyme on a pyrolytic graphite electrode, more than doubling its electrocatalytic activity relative to the current obtained by simple adsorption of the protein to the carbon surface.

PubMed: 21544308
DOI: 10.1039/C0DT01403F

実験手法

X-RAY DIFFRACTION (2.305 Å)