7DHQ
Structure of Halothiobacillus neapolitanus Microcompartments Protein CsoS1D
Summary for 7DHQ
| Entry DOI | 10.2210/pdb7dhq/pdb |
| Descriptor | Microcompartments protein (2 entities in total) |
| Functional Keywords | microcompartments protein, csos1d, structural protein |
| Biological source | Halothiobacillus neapolitanus (strain ATCC 23641 / c2) |
| Total number of polymer chains | 6 |
| Total formula weight | 150681.47 |
| Authors | Xue, B.,Tan, Y.Q.,Ali, S.,Robinson, R.C.,Narita, A.,Yew, W.S. (deposition date: 2020-11-17, release date: 2021-08-25, Last modification date: 2023-11-29) |
| 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 | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
Download full validation report
