6N63

Crystal structure of an Iron binding protein

6N63 の概要

• エントリーDOI: 10.2210/pdb6n63/pdb
• 分子名称: ENCAPSULIN CARGO PROTEIN, GLYCOLIC ACID, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: iron storage, mineralization, encapsulin, ferroxidase, metal binding protein
• 由来する生物種: Bacillus thermotolerans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23661.94

構造登録者

Birrane, G.,Geissen, T.W. (登録日: 2018-11-24, 公開日: 2019-07-17, 最終更新日: 2024-04-03)

主引用文献

Giessen, T.W.,Orlando, B.J.,Verdegaal, A.A.,Chambers, M.G.,Gardener, J.,Bell, D.C.,Birrane, G.,Liao, M.,Silver, P.A.
Large protein organelles form a new iron sequestration system with high storage capacity.
Elife, 8:-, 2019

PubMed Abstract: 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.

PubMed: 31282860
DOI: 10.7554/eLife.46070

実験手法

X-RAY DIFFRACTION (1.72 Å)