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Cryo-EM structure of Mycobacterium smegmatis DyP-loaded encapsulin.


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.

SUBMITTER: Tang Y 

PROVIDER: S-EPMC8072242 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature

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Cryo-EM structure of <i>Mycobacterium smegmatis</i> DyP-loaded encapsulin.

Tang Yanting Y   Mu An A   Zhang Yuying Y   Zhou Shan S   Wang Weiwei W   Lai Yuezheng Y   Zhou Xiaoting X   Liu Fengjiang F   Yang Xiuna X   Gong Hongri H   Wang Quan Q   Rao Zihe Z  

Proceedings of the National Academy of Sciences of the United States of America 20210401 16


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 <i>Mycobacterium smegmatis</i> 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 D  ...[more]

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