Publication Type:Journal Article
Source:Biomacromolecules, Volume 13, Number 1, p.98-105 (2011)
ISBN:1526-4602 (Electronic)<br/>1525-7797 (Linking)
Keywords:Bacterial Proteins/*chemistry/genetics, Iron/*chemistry, Magnetite Nanoparticles/*chemistry/ultrastructure, Mutation, Particle Size, Protein Stability, Protein Structure, Tertiary
<p>Highly ordered mineralized structures created by living organisms are often hierarchical in structure with fundamental structural elements at nanometer scales. Proteins have been found responsible for forming many of these structures, but the mechanisms by which these biomineralization proteins function are generally poorly understood. To better understand its role in biomineralization, the magnetotactic bacterial protein, Mms6, which promotes the formation in vitro of superparamagnetic magnetite nanoparticles of uniform size and shape, was studied for its structure and function. Mms6 is shown to have two phases of iron binding: one high affinity and stoichiometric and the other low affinity, high capacity, and cooperative with respect to iron. The protein is amphipathic with a hydrophobic N-terminal domain and hydrophilic C-terminal domain. It self-assembles to form a micelle, with most particles consisting of 20-40 monomers, with the hydrophilic C-termini exposed on the outside. Studies of proteins with mutated C-terminal domains show that the C-terminal domain contributes to the stability of this multisubunit particle and binds iron by a mechanism that is sensitive to the arrangement of carboxyl/hydroxyl groups in this domain.</p>
Wang, Lijun<br/>Prozorov, Tanya<br/>Palo, Pierre E<br/>Liu, Xunpei<br/>Vaknin, David<br/>Prozorov, Ruslan<br/>Mallapragada, Surya<br/>Nilsen-Hamilton, Marit<br/>Biomacromolecules. 2012 Jan 9;13(1):98-105. doi: 10.1021/bm201278u. Epub 2011 Dec 9.