6NER
Synthetic Haliangium ochraceum BMC shell
Summary for 6NER
| Entry DOI | 10.2210/pdb6ner/pdb |
| Descriptor | BMC-H tandem fusion protein, SULFATE ION (2 entities in total) |
| Functional Keywords | bacterial microcompartment, structural protein |
| Biological source | Haliangium ochraceum More |
| Total number of polymer chains | 30 |
| Total formula weight | 655950.99 |
| Authors | Sutter, M.,McGuire, S.,Aussignargues, C.,Kerfeld, C.A. (deposition date: 2018-12-18, release date: 2019-04-03, Last modification date: 2023-10-11) |
| Primary citation | Sutter, M.,McGuire, S.,Ferlez, B.,Kerfeld, C.A. Structural Characterization of a Synthetic Tandem-Domain Bacterial Microcompartment Shell Protein Capable of Forming Icosahedral Shell Assemblies. ACS Synth Biol, 8:668-674, 2019 Cited by PubMed Abstract: Bacterial microcompartments are subcellular compartments found in many prokaryotes; they consist of a protein shell that encapsulates enzymes that perform a variety of functions. The shell protects the cell from potentially toxic intermediates and colocalizes enzymes for higher efficiency. Accordingly, it is of considerable interest for biotechnological applications. We have previously structurally characterized an intact 40 nm shell comprising three different types of proteins. One of those proteins, BMC-H, forms a cyclic hexamer; here we have engineered a synthetic protein that consists of a tandem duplication of BMC-H connected by a short linker. The synthetic protein forms cyclic trimers that self-assemble to form a smaller (25 nm) icosahedral shell with gaps at the pentamer positions. When coexpressed in vivo with the pentamer fused to an affinity tag we can purify complete icosahedral shells. This engineered shell protein constitutes a minimal shell system to study permeability; reducing symmetry from 6- to 3-fold will allow for finer control of the pore environment. We have determined a crystal structure of this shell to guide rational engineering of this microcompartment shell for biotechnological applications. PubMed: 30901520DOI: 10.1021/acssynbio.9b00011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.59 Å) |
Structure validation
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