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Issue 16, 2017
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NMR studies of the interactions between AMB-1 Mms6 protein and magnetosome Fe3O4 nanoparticles

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Abstract

Mms6 protein from magnetotactic bacteria strain AMB-1 is responsible for controlling the formation of magnetite nanoparticles both in vitro and in vivo. High-resolution NMR studies showed the C-terminal DEEVE motif and the following residues undergoing conformation change upon magnetosome Fe3O4 crystal binding. The N-terminal hydrophobic packing of Mms6 protein is important for arranging the DEEVE motifs into a correct assembly and orientation that are crucial for magnetite crystal recognition.

Graphical abstract: NMR studies of the interactions between AMB-1 Mms6 protein and magnetosome Fe3O4 nanoparticles

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Supplementary files

Article information


Submitted
28 Feb 2017
Accepted
17 Mar 2017
First published
22 Mar 2017

J. Mater. Chem. B, 2017,5, 2888-2895
Article type
Paper

NMR studies of the interactions between AMB-1 Mms6 protein and magnetosome Fe3O4 nanoparticles

K. Ma, H. Zhao, X. Zheng, H. Sun, L. Hu, L. Zhu, Y. Shen, T. Luo, H. Dai and J. Wang, J. Mater. Chem. B, 2017, 5, 2888
DOI: 10.1039/C7TB00570A

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