5z8j | pdb_00005z8j
Human mitochondrial ferritin mutant - E27C/E62C/C102G/C130G
Structural highlights
Function[FTMT_HUMAN] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.[1] [2] Publication Abstract from PubMedBACKGROUND: Protein nanocages have emerged as popular nanocarriers for either drug delivery or biotemplates for the preparation of nanomaterials. However, only three interfaces, namely exterior surface, intersubunit and inner cavity, have been used as reaction sites for the above purposes with all known protein nanocages. On the other hand, how to control the site of Au NCs formed within a targeted protein template while maintaining the functionality of protein itself remains challenging. RESULTS: In this work, inspired by compartmentalization in living systems, we firstly come up with the conception of "intrasubunit interfaces", located within subunit of protein nanocage. We built a new, specific compartment for fabrication of gold nanoclusters by genetic modification of the inherent ferroxidase center located within four-alpha-helix bundle of each ferritin subunit. This newly built compartment not only realizes the site-directed synthesis of gold nanoclusters but also has no effect on the functionality of ferritin itself such as encapsulation by its inner cavity. These redesigned composites can be further applied as fluorescent imaging agent and carriers for preparation of hybrid nanomaterials. CONCLUSIONS: The designing strategy of intrasubunit interfaces opens a new way for future applications of cage-like proteins. Design and site-directed compartmentalization of gold nanoclusters within the intrasubunit interfaces of ferritin nanocage.,Zang J, Zheng B, Zhang X, Arosio P, Zhao G J Nanobiotechnology. 2019 Jul 5;17(1):79. doi: 10.1186/s12951-019-0512-0. PMID:31277668[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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