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| Title | Cryo-EM structure of a thermostable bacterial nanocompartment. |
|---|---|
| Journal, issue, pages | IUCrJ, Vol. 8, Issue Pt 3, Page 342-350, Year 2021 |
| Publish date | May 1, 2021 |
 Authors | Timothy Wiryaman / Navtej Toor /  |
| PubMed Abstract | Protein nanocompartments are widespread in bacteria and archaea, but their functions are not yet well understood. Here, the cryo-EM structure of a nanocompartment from the thermophilic bacterium is ...Protein nanocompartments are widespread in bacteria and archaea, but their functions are not yet well understood. Here, the cryo-EM structure of a nanocompartment from the thermophilic bacterium is reported at 2.0 Å resolution. The high resolution of this structure shows that interactions in the E-loop domain may be important for the thermostability of the nanocompartment assembly. Also, the channels at the fivefold axis, threefold axis and dimer interface are assessed for their ability to transport iron. Finally, an unexpected flavin ligand was identified on the exterior of the shell, indicating that this nanocompartment may also play a direct role in iron metabolism. |
 External links | IUCrJ / PubMed:33953921 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.0 Å |
| Structure data | EMDB-22992, PDB-7kq5: |
| Chemicals |  ChemComp-FMN:  ChemComp-HOH: |
| Source |
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 Keywords |  VIRUS LIKE PARTICLE / Encapsulin / HK97 fold / flavin-binding / icosahedral |
