Cryo-EM structure of <i>Mycobacterium smegmatis</i> DyP-loaded encapsulin
Yanting Tang, A. Mu, Yuying Zhang, Shan Zhou, Weiwei Wang, Yuezheng Lai, Xiaoting Zhou, Fengjiang Liu, Xiuna Yang, Hongri Gong, Quan Wang, Zihe Rao
Abstract
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.