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-Structure paper
Title | Cryo-EM structure of DyP-loaded encapsulin. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 118, Issue 16, Year 2021 |
Publish date | Apr 20, 2021 |
![]() | Yanting Tang / An Mu / Yuying Zhang / Shan Zhou / Weiwei Wang / Yuezheng Lai / Xiaoting Zhou / Fengjiang Liu / Xiuna Yang / Hongri Gong / Quan Wang / Zihe Rao / ![]() |
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 ...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. |
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Methods | EM (single particle) |
Resolution | 2.5 - 4.1 Å |
Structure data | EMDB-30130, PDB-7boj: EMDB-30131, PDB-7bok: ![]() EMDB-30132: |
Chemicals | ![]() ChemComp-HEM: |
Source |
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