Cryo-EM structure of Mycobacterium smegmatis DyP-loaded encapsulin.
Proc Natl Acad Sci U S A
; 118(16)2021 04 20.
Article
em En
| MEDLINE
| ID: mdl-33853951
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 Mycobacterium smegmatis 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.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Peroxidases
/
Proteínas de Bactérias
/
Mycobacterium smegmatis
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article