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7KQ5

Cryo-EM structure of a thermostable encapsulin from T. maritima

Summary for 7KQ5
Entry DOI10.2210/pdb7kq5/pdb
EMDB information22992
DescriptorMaritimacin, FLAVIN MONONUCLEOTIDE (3 entities in total)
Functional Keywordsencapsulin, hk97 fold, flavin-binding, icosahedral, virus like particle
Biological sourceThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Total number of polymer chains1
Total formula weight30973.13
Authors
Wiryaman, T.I.,Toor, N. (deposition date: 2020-11-13, release date: 2021-04-28, Last modification date: 2024-03-06)
Primary citationWiryaman, T.,Toor, N.
Cryo-EM structure of a thermostable bacterial nanocompartment.
Iucrj, 8:342-350, 2021
Cited by
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 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.
PubMed: 33953921
DOI: 10.1107/S2052252521001949
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2 Å)
Structure validation

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