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DNA Self-Assembly: From Chirality to Evolution
Int. J. Mol. Sci. 2013, 14(7), 14594-14606; doi:10.3390/ijms140714594

Integrated Self-Assembly of the Mms6 Magnetosome Protein to Form an Iron-Responsive Structure

1 Ames National Laboratory, Ames, IA 50011, USA 2 Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA 3 Department of Chemical and Biological Engineering, Iowa State University, Ames, IA 50011, USA Current address: National Center for Protein Science Shanghai, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 333 Haike Road, Shanghai 201203, China;
* Author to whom correspondence should be addressed.
Received: 5 February 2013 / Revised: 9 June 2013 / Accepted: 3 July 2013 / Published: 12 July 2013
(This article belongs to the Special Issue Molecular Self-Assembly 2012)
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A common feature of biomineralization proteins is their self-assembly to produce a surface consistent in size with the inorganic crystals that they produce. Mms6, a small protein of 60 amino acids from Magnetospirillum magneticum strain AMB-1 that promotes the in vitro growth of superparamagnetic magnetite nanocrystals, assembles in aqueous solution to form spherical micelles that could be visualized by TEM and AFM. The results reported here are consistent with the view that the N and C-terminal domains interact with each other within one polypeptide chain and across protein units in the assembly. From studies to determine the amino acid residues important for self-assembly, we identified the unique GL repeat in the N-terminal domain with additional contributions from amino acids in other positions, throughout the molecule. Analysis by CD spectroscopy identified a structural change in the iron-binding C-terminal domain in the presence of Fe3+. A change in the intrinsic fluorescence of tryptophan in the N-terminal domain showed that this structural change is transmitted through the protein. Thus, self-assembly of Mms6 involves an interlaced structure of intra- and inter-molecular interactions that results in a coordinated structural change in the protein assembly with iron binding.
Keywords: Mms6; micelle; structural rearrangement Mms6; micelle; structural rearrangement
This is an open access article distributed under the Creative Commons Attribution License (CC BY) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Feng, S.; Wang, L.; Palo, P.; Liu, X.; Mallapragada, S.K.; Nilsen-Hamilton, M. Integrated Self-Assembly of the Mms6 Magnetosome Protein to Form an Iron-Responsive Structure. Int. J. Mol. Sci. 2013, 14, 14594-14606.

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