7BOK

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

Summary for 7BOK

• Entry DOI: 10.2210/pdb7bok/pdb
• EMDB information: 30130 30131 30132
• Descriptor: Dyp-type peroxidase, PROTOPORPHYRIN IX CONTAINING FE (2 entities in total)
• Functional Keywords: cargo protein, dodecamer, heme-containing enzyme, oxidoreductase
• Biological source: Mycolicibacterium smegmatis MC2 155
• Total number of polymer chains: 6
• Total formula weight: 227212.96

Authors

Tang, Y.T.,Mu, A.,Gong, H.R.,Wang, Q.,Rao, Z.H. (deposition date: 2020-03-19, release date: 2021-03-24, Last modification date: 2024-03-27)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.7 Å)