Cryo-EM Structure of Heterologous Protein Complex Loaded Thermotoga Maritima Encapsulin Capsid

Biomolecules

卷:10

FrankS. Vago¹  Chen Sun¹  Thomas Klose¹  Wen Jiang¹  Jiankang Zhu²  Xiansong Xiong³ 

[1] Department of Biological Sciences, Markey Center for Structural Biology, Purdue University, West Lafayette, IN 47906, USA;

[2] Shanghai Center for Plant Stress Biology, Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai 201602, China;

[3] University of Chinese Academy of Sciences, Beijing 100864, China;

关键词: cryo-EM;    encapsulin;    baculovirus expression system;    cargo-loading peptide;    complex assembly;   

DOI  :  10.3390/biom10091342

来源: DOAJ

【 摘 要 】

Encapsulin is a class of nanocompartments that is unique in bacteria and archaea to confine enzymatic activities and sequester toxic reaction products. Here we present a 2.87 Å resolution cryo-EM structure of Thermotoga maritima encapsulin with heterologous protein complex loaded. It is the first successful case of expressing encapsulin and heterologous cargo protein in the insect cell system. Although we failed to reconstruct the cargo protein complex structure due to the signal interference of the capsid shell, we were able to observe some unique features of the cargo-loaded encapsulin shell, for example, an extra density at the fivefold pore that has not been reported before. These results would lead to a more complete understanding of the encapsulin cargo assembly process of T. maritima.

【 授权许可】

Unknown