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7CKC

Simplified Alpha-Carboxysome, T=4

This is a non-PDB format compatible entry.
Summary for 7CKC
Entry DOI10.2210/pdb7ckc/pdb
EMDB information30385
DescriptorUnidentified carboxysome polypeptide, Major carboxysome shell protein 1A (2 entities in total)
Functional Keywordsbacterial microcompartment, alpha-carboxysome, virus like particle
Biological sourceHalothiobacillus neapolitanus
More
Total number of polymer chains240
Total formula weight2405644.44
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 citationTan, 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: 34384019
DOI: 10.1021/acs.biomac.1c00533
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.9 Å)
Structure validation

237735

數據於2025-06-18公開中

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