7BOK

Cryo-EM structure of the encapsulated DyP-type peroxidase from Mycobacterium smegmatis

7BOK の概要

• エントリーDOI: 10.2210/pdb7bok/pdb
• EMDBエントリー: 30130 30131 30132
• 分子名称: Dyp-type peroxidase, PROTOPORPHYRIN IX CONTAINING FE (2 entities in total)
• 機能のキーワード: cargo protein, dodecamer, heme-containing enzyme, oxidoreductase
• 由来する生物種: Mycolicibacterium smegmatis MC2 155
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 227212.96

構造登録者

Tang, Y.T.,Mu, A.,Gong, H.R.,Wang, Q.,Rao, Z.H. (登録日: 2020-03-19, 公開日: 2021-03-24, 最終更新日: 2024-03-27)

主引用文献

Tang, Y.,Mu, A.,Zhang, Y.,Zhou, S.,Wang, W.,Lai, Y.,Zhou, X.,Liu, F.,Yang, X.,Gong, H.,Wang, Q.,Rao, Z.
Cryo-EM structure of Mycobacterium smegmatis DyP-loaded encapsulin.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: Encapsulins containing dye-decolorizing peroxidase (DyP)-type peroxidases are ubiquitous among prokaryotes, protecting cells against oxidative stress. However, little is known about how they interact and function. Here, we have isolated a native cargo-packaging encapsulin from and determined its complete high-resolution structure by cryogenic electron microscopy (cryo-EM). This encapsulin comprises an icosahedral shell and a dodecameric DyP cargo. The dodecameric DyP consists of two hexamers with a twofold axis of symmetry and stretches across the interior of the encapsulin. Our results reveal that the encapsulin shell plays a role in stabilizing the dodecameric DyP. Furthermore, we have proposed a potential mechanism for removing the hydrogen peroxide based on the structural features. Our study also suggests that the DyP is the primary cargo protein of mycobacterial encapsulins and is a potential target for antituberculosis drug discovery.

PubMed: 33853951
DOI: 10.1073/pnas.2025658118

実験手法

ELECTRON MICROSCOPY (3.7 Å)