Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 118, Issue 16, Pages -Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2025658118
Keywords
encapsulin nanocompartment; dye-decolorizing peroxidase; cryo-electron microscopy; Mycobacterium smegmatis
Categories
Funding
- National Key Research and Development Program of China [2017YFC0840300, 2020YFA0707500]
- Strategic Priority Research Program of the CAS [XDB08020200, XDB37020203]
- National Natural Science Foundation of China [81520108019, 813300237, 31971118]
- Tianjin Natural Science Foundation [20JCQNJC01430]
- Science and Technology Commission of Shanghai Municipality [YDZX20203100001571]
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Encapsulins containing dye-decolorizing peroxidase (DyP)-type peroxidases play a role in protecting prokaryotic cells against oxidative stress. Through isolating and studying a native cargo-packaging encapsulin from Mycobacterium smegmatis, researchers have determined the high-resolution structure and proposed a potential mechanism for hydrogen peroxide removal. The study suggests DyP as the primary cargo protein of mycobacterial encapsulins and a potential target for antituberculosis drug discovery.
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.
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