Deciphering molecular details in the assembly of alpha-type carboxysome

Yilan Liu, Xinyuan He, Weiping Lim, Joshua Mueller, Justin Lawrie, Levi Kramer, Jiantao Guo, Wei Niu

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


Bacterial microcompartments (BMCs) are promising natural protein structures for applications that require the segregation of certain metabolic functions or molecular species in a defined microenvironment. To understand how endogenous cargos are packaged inside the protein shell is key for using BMCs as nano-scale reactors or delivery vesicles. In this report, we studied the encapsulation of RuBisCO into the α-type carboxysome from Halothiobacillus neapolitan. Our experimental data revealed that the CsoS2 scaffold proteins engage RuBisCO enzyme through an interaction with the small subunit (CbbS). In addition, the N domain of the large subunit (CbbL) of RuBisCO interacts with all shell proteins that can form the hexamers. The binding affinity between the N domain of CbbL and one of the major shell proteins, CsoS1C, is within the submicromolar range. The absence of the N domain also prevented the encapsulation of the rest of the RuBisCO subunits. Our findings complete the picture of how RuBisCOs are encapsulated into the α-type carboxysome and provide insights for future studies and engineering of carboxysome as a protein shell.

Original languageEnglish (US)
Article number15062
JournalScientific reports
Issue number1
StatePublished - Dec 1 2018

ASJC Scopus subject areas

  • General


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