7K5W

Cryo-EM structure of heterologous protein complex loaded Thermotoga maritima encapsulin capsid

Summary for 7K5W

• Entry DOI: 10.2210/pdb7k5w/pdb
• EMDB information: 22617
• Descriptor: Maritimacin (1 entity in total)
• Functional Keywords: encapsulin, baculovirus expression system, cargo loading peptide, complex assembly, metal binding protein, hydrolase
• Biological source: Thermotoga maritima
• Total number of polymer chains: 1
• Total formula weight: 31489.79

Authors

Xiong, X.,Sun, C.,Vago, F.S.,Klose, T.,Zhu, J.,Jiang, W. (deposition date: 2020-09-17, release date: 2020-10-07, Last modification date: 2024-03-06)

Primary citation

Xiong, X.,Sun, C.,Vago, F.S.,Klose, T.,Zhu, J.,Jiang, W.
Cryo-EM Structure of Heterologous Protein Complex Loaded Thermotoga Maritima Encapsulin Capsid.
Biomolecules, 10:-, 2020

PubMed Abstract: 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 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 .

PubMed: 32961724
DOI: 10.3390/biom10091342

Experimental method

ELECTRON MICROSCOPY (2.87 Å)