7DL5

Crystal structure of Thermotoga Maritima ferritin mutant at 2.3 Angstrom resolution

Summary for 7DL5

• Entry DOI: 10.2210/pdb7dl5/pdb
• Descriptor: Ferritin, FE (III) ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: metal binding protein
• Biological source: Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
• Total number of polymer chains: 2
• Total formula weight: 34864.29

Authors

Liu, Y.,Leng, X.,Zang, J.,Zhao, G. (deposition date: 2020-11-26, release date: 2021-12-01, Last modification date: 2023-11-29)

Primary citation

Liu, Y.,Zang, J.,Leng, X.,Zhao, G.
A short helix regulates conversion of dimeric and 24-meric ferritin architectures.
Int.J.Biol.Macromol., 203:535-542, 2022

PubMed Abstract: The inter-subunit interaction at the protein interfaces plays a key role in protein self-assembly, through which enabling protein self-assembly controllable is of great importance for preparing the novel nanoscale protein materials with unexplored properties. Different from normal 24-meric ferritin, archaeal ferritin, Thermotoga maritima ferritin (TmFtn) naturally occurs as a dimer, which can assemble into a 24-mer nanocage induced by salts. However, the regulation mechanism of protein self-assembly underlying this phenomenon remains unclear. Here, a combination of the computational energy simulation and key interface reconstruction revealed that a short helix involved interactions at the C interface are mainly responsible for the existence of such dimer. Agreeing with this idea, deletion of such short helix of each subunit triggers it to be a stable dimer, which losses the ability to reassemble into 24-meric ferritin in the presence of salts in solution. Further support for this idea comes from the observation that grafting a small helix from human H ferritin onto archaeal subunit resulted in a stable 24-mer protein nanocage even in the absence of salts. Thus, these findings demonstrate that adjusting the interactions at the protein interfaces appears to be a facile, effective approach to control subunit assembly into different protein architectures.

PubMed: 35120932
DOI: 10.1016/j.ijbiomac.2022.01.174

Experimental method

X-RAY DIFFRACTION (2.3 Å)