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Cryo-EM structure of a thermostable bacterial nanocompartment.

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 Thermotoga maritima 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.

SUBMITTER: Wiryaman T

PROVIDER: S-EPMC8086157 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature

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Cryo-EM structure of a thermostable bacterial nanocompartment.

Wiryaman Timothy T Toor Navtej N

IUCrJ 20210402 Pt 3

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 <i>Thermotoga maritima</i> 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 ...[more]

PMID: 33953921

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