8BBQ

Determination of the structure of active tyrosinase from bacterium Verrucomicrobium spinosum

8BBQ の概要

• エントリーDOI: 10.2210/pdb8bbq/pdb
• 分子名称: Core tyrosinase, GLYCEROL, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: tyrosinase, copper, verrucomicrobium spinosum, ppo, metal binding protein
• 由来する生物種: Verrucomicrobium spinosum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74606.64

構造登録者

Fekry, M.,Dave, K.,Badgujar, D.,Aurelius, O.,Hamnevik, E.,Dobritzsch, D.,Danielson, H. (登録日: 2022-10-14, 公開日: 2023-09-20, 最終更新日: 2023-10-11)

主引用文献

Fekry, M.,Dave, K.K.,Badgujar, D.,Hamnevik, E.,Aurelius, O.,Dobritzsch, D.,Danielson, U.H.
The Crystal Structure of Tyrosinase from Verrucomicrobium spinosum Reveals It to Be an Atypical Bacterial Tyrosinase.
Biomolecules, 13:-, 2023

PubMed Abstract: Tyrosinases belong to the type-III copper enzyme family, which is involved in melanin production in a wide range of organisms. Despite similar overall characteristics and functions, their structures, activities, substrate specificities and regulation vary. The tyrosinase from the bacterium (Tyr) is produced as a pre-pro-enzyme in which a C-terminal extension serves as an inactivation domain. It does not require a caddie protein for copper ion incorporation, which makes it similar to eukaryotic tyrosinases. To gain an understanding of the catalytic machinery and regulation of Tyr activity, we determined the structure of the catalytically active "core domain" of Tyr by X-ray crystallography. The analysis showed that Tyr is an atypical bacterial tyrosinase not only because it is independent of a caddie protein but also because it shows the highest structural (and sequence) similarity to plant-derived members of the type-III copper enzyme family and is more closely related to fungal tyrosinases regarding active site features. By modelling the structure of the pre-pro-enzyme using AlphaFold, we observed that Phe453, located in the C-terminal extension, is appropriately positioned to function as a "gatekeeper" residue. Our findings raise questions concerning the evolutionary origin of Tyr.

PubMed: 37759761
DOI: 10.3390/biom13091360

実験手法

X-RAY DIFFRACTION (1.43 Å)