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TitleCryo-EM Structure of Heterologous Protein Complex Loaded Encapsulin Capsid.
Journal, issue, pagesBiomolecules, Vol. 10, Issue 9, Year 2020
Publish dateSep 19, 2020
AuthorsXiansong Xiong / Chen Sun / Frank S Vago / Thomas Klose / Jiankang Zhu / Wen Jiang /
PubMed AbstractEncapsulin 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 ...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 .
External linksBiomolecules / PubMed:32961724 / PubMed Central
MethodsEM (single particle)
Resolution2.86 - 2.87 Å
Structure data

22617

7k5w

EMDB-22617, PDB-7k5w:
Cryo-EM structure of heterologous protein complex loaded Thermotoga maritima encapsulin capsid
Method: EM (single particle) / Resolution: 2.86 Å

Source
  • thermotoga maritima (bacteria)
KeywordsHYDROLASE / encapsulin / baculovirus expression system / cargo loading peptide / complex assembly / METAL BINDING PROTEIN

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