6TXM

Crystal structure of thermotoga maritima E65R Ferritin

Summary for 6TXM

• Entry DOI: 10.2210/pdb6txm/pdb
• Descriptor: Ferritin, SULFATE ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: metal binding, engineered protein, metal binding protein
• Biological source: Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
• Total number of polymer chains: 8
• Total formula weight: 160072.28

Authors

Wilk, P.,Grudnik, P.,Kumar, M.,Heddle, J.,Chakraborti, S. (deposition date: 2020-01-14, release date: 2021-07-28, Last modification date: 2024-01-24)

Primary citation

Kumar, M.,Markiewicz-Mizera, J.,Janna Olmos, J.D.,Wilk, P.,Grudnik, P.,Biela, A.P.,Jemiola-Rzeminska, M.,Gorecki, A.,Chakraborti, S.,Heddle, J.G.
A single residue can modulate nanocage assembly in salt dependent ferritin.
Nanoscale, 13:11932-11942, 2021

PubMed Abstract: Cage forming proteins have numerous potential applications in biomedicine and biotechnology, where the iron storage ferritin is a widely used example. However, controlling ferritin cage assembly/disassembly remains challenging, typically requiring extreme conditions incompatible with many desirable cargoes, particularly for more fragile biopharmaceuticals. Recently, a ferritin from the hyperthermophile bacterium Thermotoga maritima (TmFtn) has been shown to have reversible assembly under mild conditions, offering greater potential biocompatibility in terms of cargo access and encapsulation. Like Archeoglobus fulgidus ferritin (AfFtn), TmFtn forms 24mer cages mediated by metal ions (Mg2+). We have solved the crystal structure of the wild type TmFtn and several mutants displaying different assembly/disassembly properties. These data combined with other biophysical studies allow us to suggest candidate interfacial amino acids crucial in controlling assembly. This work deepens our understanding of how these ferritin complexes assemble and is a useful step towards production of triggerable ferritins in which these properties can be finely designed and controlled.

PubMed: 34195748
DOI: 10.1039/d1nr01632f

Experimental method

X-RAY DIFFRACTION (2.198 Å)