Summary for 7CKC
Entry DOI | 10.2210/pdb7ckc/pdb |
EMDB information | 30385 |
Descriptor | Unidentified carboxysome polypeptide, Major carboxysome shell protein 1A (2 entities in total) |
Functional Keywords | bacterial microcompartment, alpha-carboxysome, virus like particle |
Biological source | Halothiobacillus neapolitanus More |
Total number of polymer chains | 240 |
Total formula weight | 2405644.44 |
Authors | Tan, Y.Q.,Ali, S.,Xue, B.,Robinson, R.C.,Narita, A.,Yew, W.S. (deposition date: 2020-07-16, release date: 2021-08-25, Last modification date: 2024-05-29) |
Primary citation | Tan, Y.Q.,Ali, S.,Xue, B.,Teo, W.Z.,Ling, L.H.,Go, M.K.,Lv, H.,Robinson, R.C.,Narita, A.,Yew, W.S. Structure of a Minimal alpha-Carboxysome-Derived Shell and Its Utility in Enzyme Stabilization. Biomacromolecules, 22:4095-4109, 2021 Cited by PubMed 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 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. PubMed: 34384019DOI: 10.1021/acs.biomac.1c00533 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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