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Surface tubular elements (STEs) are critical components of poxvirus mature virions and play a role in suppressing host cell protein synthesis. In this study, we isolated and purified STEs from native poxvirus virions and subsequently determined their core composition and high-resolution architecture. We identified that STE is mainly composed of membrane proteins A14 and A17, along with phospholipid molecules. Within the repeat structural unit of STE, A14 proteins form two homodimers within the repeating unit, with A17 monomers flanking either side. Phospholipid molecules are distributed within the A14-A14 and A14-A17 interfaces. Our study not only revealed the molecular structures of A14 and A17 but also further emphasized that the reticulon-like and highly oligomerized characteristics of A17 provide membrane curvature, while the A14-A17-phospholipid network stabilizes the tubular structure. We proposed a hypothetical model that A17 drives changes in viral membrane curvature during maturation. These findings enhance our understanding of poxvirus biology and may guide therapeutic strategies against poxvirus infections.