6I3L

Bilirubin oxidase from Myrothecium verrucaria, mutant W396F

Summary for 6I3L

• Entry DOI: 10.2210/pdb6i3l/pdb
• Related: 6I3J 6I3K
• Descriptor: Bilirubin oxidase, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• Functional Keywords: enzymatic activity, mutant, oxidoreductase
• Biological source: Albifimbria verrucaria
• Total number of polymer chains: 2
• Total formula weight: 123859.74

Authors

Koval, T.,Svecova, L.,Skalova, T.,Kolenko, P.,Duskova, J.,Ostergaard, L.H.,Dohnalek, J. (deposition date: 2018-11-06, release date: 2019-10-02, Last modification date: 2024-10-23)

Primary citation

Koval, T.,Svecova, L.,Ostergaard, L.H.,Skalova, T.,Duskova, J.,Hasek, J.,Kolenko, P.,Fejfarova, K.,Stransky, J.,Trundova, M.,Dohnalek, J.
Trp-His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer.
Sci Rep, 9:13700-13700, 2019

PubMed Abstract: Unlike any protein studied so far, the active site of bilirubin oxidase from Myrothecium verrucaria contains a unique type of covalent link between tryptophan and histidine side chains. The role of this post-translational modification in substrate binding and oxidation is not sufficiently understood. Our structural and mutational studies provide evidence that this Trp396-His398 adduct modifies T1 copper coordination and is an important part of the substrate binding and oxidation site. The presence of the adduct is crucial for oxidation of substituted phenols and it substantially influences the rate of oxidation of bilirubin. Additionally, we bring the first structure of bilirubin oxidase in complex with one of its products, ferricyanide ion, interacting with the modified tryptophan side chain, Arg356 and the active site-forming loop 393-398. The results imply that structurally and chemically distinct types of substrates, including bilirubin, utilize the Trp-His adduct mainly for binding and to a smaller extent for electron transfer.

PubMed: 31548583
DOI: 10.1038/s41598-019-50105-3

Experimental method

X-RAY DIFFRACTION (2.1 Å)