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TitleLarge protein organelles form a new iron sequestration system with high storage capacity.
Journal, issue, pagesElife, Vol. 8, Year 2019
Publish dateJul 8, 2019
AuthorsTobias W Giessen / Benjamin J Orlando / Andrew A Verdegaal / Melissa G Chambers / Jules Gardener / David C Bell / Gabriel Birrane / Maofu Liao / Pamela A Silver /
PubMed AbstractIron storage proteins are essential for cellular iron homeostasis and redox balance. Ferritin proteins are the major storage units for bioavailable forms of iron. Some organisms lack ferritins, and ...Iron storage proteins are essential for cellular iron homeostasis and redox balance. Ferritin proteins are the major storage units for bioavailable forms of iron. Some organisms lack ferritins, and it is not known how they store iron. Encapsulins, a class of protein-based organelles, have recently been implicated in microbial iron and redox metabolism. Here, we report the structural and mechanistic characterization of a 42 nm two-component encapsulin-based iron storage compartment from . Using cryo-electron microscopy and x-ray crystallography, we reveal the assembly principles of a thermostable T = 4 shell topology and its catalytic ferroxidase cargo and show interactions underlying cargo-shell co-assembly. This compartment has an exceptionally large iron storage capacity storing over 23,000 iron atoms. Our results reveal a new approach for survival in diverse habitats with limited or fluctuating iron availability via an iron storage system able to store 10 to 20 times more iron than ferritin.
External linksElife / PubMed:31282860 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.72 - 3.85 Å
Structure data

9383

6nj8

EMDB-9383, PDB-6nj8:
Encapsulin iron storage compartment from Quasibacillus thermotolerans
Method: EM (single particle) / Resolution: 3.85 Å

PDB-6n63:
Crystal structure of an Iron binding protein
Method: X-RAY DIFFRACTION / Resolution: 1.72 Å

Chemicals

ChemComp-GOA:
GLYCOLIC ACID / Glycolic acid

ChemComp-ACT:
ACETATE ION / Acetate

ChemComp-FE:
Unknown entry / Iron

ChemComp-HOH:
WATER / Water

Source
  • bacillus thermotolerans (bacteria)
  • quasibacillus thermotolerans (bacteria)
KeywordsMETAL BINDING PROTEIN / IRON STORAGE / MINERALIZATION / ENCAPSULIN / FERROXIDASE / METAL TRANSPORT / IMEF / icosahedral

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