Structure of a Minimal α-Carboxysome-Derived Shell and Its Utility in Enzyme Stabilization

Yong Quan Tan, Samson Ali, Bo Xue, Wei Zhe Teo, Lay Hiang Ling, Maybelle Kho Go, Hong Lv, Robert C. Robinson, Akihiro Narita, Wen Shan Yew

Research output: Contribution to journalArticlepeer-review

Abstract

Bacterial microcompartments are proteinaceous shells that encase specialized metabolic processes in bacteria. Recent advances in simplification of these intricate shells have encouraged bioengineering efforts. Here, we construct minimal shells derived from the Halothiobacillus neapolitanus α-carboxysome, which we term Cso-shell. Using cryogenic electron microscopy, the atomic-level structures of two shell forms were obtained, reinforcing notions of evolutionarily conserved features in bacterial microcompartment shell architecture. Encapsulation peptide sequences that facilitate loading of heterologous protein cargo within the shells were identified. We further provide a first demonstration in utilizing minimal bacterial microcompartment-derived shells for hosting heterologous enzymes. Cso-shells were found to stabilize enzymatic activities against heat shock, presence of methanol co-solvent, consecutive freeze-thawing, and alkaline environments. This study yields insights into α-carboxysome assembly and advances the utility of synthetic bacterial microcompartments as nanoreactors capable of stabilizing enzymes with varied properties and reaction chemistries.

Original languageEnglish
Pages (from-to)4095-4109
Number of pages15
JournalBiomacromolecules
Volume22
Issue number10
DOIs
Publication statusPublished - Oct 11 2021

ASJC Scopus subject areas

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

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