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-Structure paper
タイトル | Cryo-EM structure of DyP-loaded encapsulin. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 118, Issue 16, Year 2021 |
掲載日 | 2021年4月20日 |
著者 | 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 要旨 | 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. |
リンク | Proc Natl Acad Sci U S A / PubMed:33853951 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.5 - 4.1 Å |
構造データ | EMDB-30130, PDB-7boj: EMDB-30131, PDB-7bok: EMDB-30132: |
化合物 | ChemComp-HEM: |
由来 |
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キーワード | VIRUS LIKE PARTICLE / Nanocompartment / Icosahedral shell / Cargo loaded / OXIDOREDUCTASE / Cargo protein / Dodecamer / Heme-containing enzyme |