7dl5
Crystal structure of Thermotoga Maritima ferritin mutant at 2.3 Angstrom resolutionCrystal structure of Thermotoga Maritima ferritin mutant at 2.3 Angstrom resolution
Structural highlights
FunctionQ9X0L2_THEMA Iron storage protein (By similarity).[RuleBase:RU361145] Publication Abstract from PubMedThe 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 C4 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. A short helix regulates conversion of dimeric and 24-meric ferritin architectures.,Liu Y, Zang J, Leng X, Zhao G Int J Biol Macromol. 2022 Apr 1;203:535-542. doi: 10.1016/j.ijbiomac.2022.01.174., Epub 2022 Feb 2. PMID:35120932[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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