dc.contributor.author | Giessen, Tobias W. | |
dc.contributor.author | Orlando, Benjamin J. | |
dc.contributor.author | Verdegaal, Andrew A. | |
dc.contributor.author | Chambers, Melissa G. | |
dc.contributor.author | Gardener, Jules | |
dc.contributor.author | Bell, David C. | |
dc.contributor.author | Birrane, Gabriel | |
dc.contributor.author | Liao, Maofu | |
dc.contributor.author | Silver, Pamela A. | |
dc.date.accessioned | 2020-04-29T18:29:14Z | |
dc.date.available | 2020-04-29T18:29:14Z | |
dc.date.issued | 2019-07-08 | |
dc.identifier.citation | eLife 2019;8:e46070 doi: 10.7554/eLife.46070 | en_US |
dc.identifier.issn | 2050-084X | |
dc.identifier.uri | http://hdl.handle.net/1803/9984 | |
dc.description.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 Quasibacillus thermotolerans. 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. | en_US |
dc.description.sponsorship | Deutsche Akademie der Naturforscher Leopoldina - Nationale Akademie der Wissenschaften LPDS 2014-05 Tobias W Giessen
Gordon and Betty Moore Foundation 5506 Tobias W Giessen Pamela A Silver
Wyss Institute for Biologically Inspired Engineering Tobias W Giessen Pamela A Silver
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | eLife | en_US |
dc.rights | © 2019, Giessen et al.
This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited. | |
dc.source.uri | https://elifesciences.org/articles/46070 | |
dc.subject | I-TASSER | en_US |
dc.subject | FERRITIN | en_US |
dc.subject | NANOCOMPARTMENT | en_US |
dc.subject | MECHANISM | en_US |
dc.subject | BACTERIOFERRITIN | en_US |
dc.subject | IMPLEMENTATION | en_US |
dc.subject | VISUALIZATION | en_US |
dc.subject | ENCAPSULIN | en_US |
dc.subject | EVOLUTION | en_US |
dc.subject | PHOSPHATE | en_US |
dc.title | Large protein organelles form a new iron sequestration system with high storage capacity | en_US |
dc.type | Article | en_US |
dc.identifier.doi | 10.7554/eLife.46070 | |